Biomineralization: Functions of calmodulin-like protein in the shell formation of pearl oyster

Calmodulin-like protein (CaLP) was believed to be involved in the shell formation of pearl oyster. However, no further study of this protein was ever performed. In this study, the in vitro crystallization experiment showed that CaLP can modify the morphology of calcite. In addition, aragonite crysta...

Full description

Saved in:
Bibliographic Details
Published inBiochimica et biophysica acta Vol. 1770; no. 9; pp. 1338 - 1344
Main Authors Yan, Zhenguang, Fang, Zi, Ma, Zhuojun, Deng, Jinye, Li, Shuo, Xie, Liping, Zhang, Rongqing
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.09.2007
Subjects
Online AccessGet full text

Cover

Loading…
Abstract Calmodulin-like protein (CaLP) was believed to be involved in the shell formation of pearl oyster. However, no further study of this protein was ever performed. In this study, the in vitro crystallization experiment showed that CaLP can modify the morphology of calcite. In addition, aragonite crystals can be induced in the mixture of CaLP and a nacre protein (at 16 kDa), which was detected and purified from the EDTA-soluble matrix of nacre. These results agreed with that of immunohistological staining in which CaLP was detected not only in the organic layer sandwiched between nacre (aragonite) and the prismatic layer (calcite), but also around the prisms of the prismatic layer. Take together, we concluded that (1) CaLP, as a component of the organic layer, can induce the nucleation of aragonite through binding with the 16-kDa protein, and (2) CaLP may regulate the growth of calcite in the prismatic layer.
AbstractList Calmodulin-like protein (CaLP) was believed to be involved in the shell formation of pearl oyster. However, no further study of this protein was ever performed. In this study, the in vitro crystallization experiment showed that CaLP can modify the morphology of calcite. In addition, aragonite crystals can be induced in the mixture of CaLP and a nacre protein (at 16 kDa), which was detected and purified from the EDTA-soluble matrix of nacre. These results agreed with that of immunohistological staining in which CaLP was detected not only in the organic layer sandwiched between nacre (aragonite) and the prismatic layer (calcite), but also around the prisms of the prismatic layer. Take together, we concluded that (1) CaLP, as a component of the organic layer, can induce the nucleation of aragonite through binding with the 16-kDa protein, and (2) CaLP may regulate the growth of calcite in the prismatic layer.Calmodulin-like protein (CaLP) was believed to be involved in the shell formation of pearl oyster. However, no further study of this protein was ever performed. In this study, the in vitro crystallization experiment showed that CaLP can modify the morphology of calcite. In addition, aragonite crystals can be induced in the mixture of CaLP and a nacre protein (at 16 kDa), which was detected and purified from the EDTA-soluble matrix of nacre. These results agreed with that of immunohistological staining in which CaLP was detected not only in the organic layer sandwiched between nacre (aragonite) and the prismatic layer (calcite), but also around the prisms of the prismatic layer. Take together, we concluded that (1) CaLP, as a component of the organic layer, can induce the nucleation of aragonite through binding with the 16-kDa protein, and (2) CaLP may regulate the growth of calcite in the prismatic layer.
Calmodulin-like protein (CaLP) was believed to be involved in the shell formation of pearl oyster. However, no further study of this protein was ever performed. In this study, the in vitro crystallization experiment showed that CaLP can modify the morphology of calcite. In addition, aragonite crystals can be induced in the mixture of CaLP and a nacre protein (at 16 kDa), which was detected and purified from the EDTA-soluble matrix of nacre. These results agreed with that of immunohistological staining in which CaLP was detected not only in the organic layer sandwiched between nacre (aragonite) and the prismatic layer (calcite), but also around the prisms of the prismatic layer. Take together, we concluded that (1) CaLP, as a component of the organic layer, can induce the nucleation of aragonite through binding with the 16-kDa protein, and (2) CaLP may regulate the growth of calcite in the prismatic layer.
Calmodulin-like protein (CaLP) was believed to be involved in the shell formation of pearl oyster. However, no further study of this protein was ever performed. In this study, the in vitro crystallization experiment showed that CaLP can modify the morphology of calcite. In addition, aragonite crystals can be induced in the mixture of CaLP and a nacre protein (at 16 kDa), which was detected and purified from the EDTA-soluble matrix of nacre. These results agreed with that of immunohistological staining in which CaLP was detected not only in the organic layer sandwiched between nacre (aragonite) and the prismatic layer (calcite), but also around the prisms of the prismatic layer. Take together, we concluded that (1) CaLP, as a component of the organic layer, can induce the nucleation of aragonite through binding with the 16-kDa protein, and (2) CaLP may regulate the growth of calcite in the prismatic layer.
Author Ma, Zhuojun
Yan, Zhenguang
Xie, Liping
Fang, Zi
Zhang, Rongqing
Deng, Jinye
Li, Shuo
Author_xml – sequence: 1
  givenname: Zhenguang
  surname: Yan
  fullname: Yan, Zhenguang
  organization: Institute of Marine Biotechnology, Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, China
– sequence: 2
  givenname: Zi
  surname: Fang
  fullname: Fang, Zi
  organization: Institute of Marine Biotechnology, Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, China
– sequence: 3
  givenname: Zhuojun
  surname: Ma
  fullname: Ma, Zhuojun
  organization: Institute of Marine Biotechnology, Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, China
– sequence: 4
  givenname: Jinye
  surname: Deng
  fullname: Deng, Jinye
  organization: Institute of Marine Biotechnology, Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, China
– sequence: 5
  givenname: Shuo
  surname: Li
  fullname: Li, Shuo
  organization: Institute of Marine Biotechnology, Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, China
– sequence: 6
  givenname: Liping
  surname: Xie
  fullname: Xie, Liping
  email: lpxie@mail.tsinghua.edu.cn
  organization: Institute of Marine Biotechnology, Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, China
– sequence: 7
  givenname: Rongqing
  surname: Zhang
  fullname: Zhang, Rongqing
  email: rqzhang@mail.tsinghua.edu.cn
  organization: Institute of Marine Biotechnology, Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, China
BackLink https://www.ncbi.nlm.nih.gov/pubmed/17692465$$D View this record in MEDLINE/PubMed
BookMark eNp9kM1u1DAURi1URKeFN0AoK3YJdhz_pAskWlFAqsQGtlg3nhvqwbEH20EqT4-nU1iwqGXJXnzn073njJyEGJCQl4x2jDL5ZtdNE3zH0PWUqo7KjjL9hGyYVn2rKZUnZEM5HdqBSXFKznLe0XrEKJ6RU6bk2A9SbMi3SxcXFzCBd7-huBgumus12MMvN3FuLPglblfvQuvdD2z2KRZ0oam33GKTb9H7Zo5puYcPxB4h-Sbe5YLpOXk6g8_44uE9J1-v33-5-tjefP7w6erdTWuHXpaWM2snmKUdp1FZxTnVk7KcQy9AA4yTHLmQQjOYR8aFAuBy0JyPveJ6tpSfk9fH3jrezxVzMYvLto4GAeOajdRMM6FEDb56CK7TgluzT26BdGf-GqmBi2PApphzwtlYV-53KwmcN4yag36zM0f95qDfUGmq_goP_8H_-h_H3h4xrIp-OUwmW4fB4tYltMVso3u84A-TkqEb
CitedBy_id crossref_primary_10_4238_2012_January_9_5
crossref_primary_10_1016_j_cbpb_2013_04_003
crossref_primary_10_1016_j_msec_2012_05_030
crossref_primary_10_2108_zsj_30_801
crossref_primary_10_1016_j_fsi_2015_04_013
crossref_primary_10_1016_j_scitotenv_2022_155114
crossref_primary_10_1186_1471_2164_11_613
crossref_primary_10_1016_j_cbd_2023_101187
crossref_primary_10_1016_j_cbpa_2018_03_007
crossref_primary_10_1371_journal_pone_0122967
crossref_primary_10_3389_fmars_2018_00203
crossref_primary_10_1021_es501638h
crossref_primary_10_1016_j_marpolbul_2012_07_043
crossref_primary_10_1002_etc_3991
crossref_primary_10_7717_peerj_10662
crossref_primary_10_1080_13235818_2024_2324466
crossref_primary_10_3389_fmars_2022_1050022
crossref_primary_10_1038_s41598_022_08610_5
crossref_primary_10_1007_s10126_022_10183_3
crossref_primary_10_1016_j_dci_2021_104180
crossref_primary_10_1007_s00438_016_1278_9
crossref_primary_10_1016_j_aquaculture_2018_04_018
crossref_primary_10_1021_bi5008854
crossref_primary_10_1016_j_fsi_2018_11_044
crossref_primary_10_3390_min7040062
crossref_primary_10_1007_s00227_013_2176_x
crossref_primary_10_1128_AEM_02737_08
crossref_primary_10_1371_journal_pone_0154279
crossref_primary_10_1371_journal_pone_0021860
crossref_primary_10_1007_s10126_012_9484_x
crossref_primary_10_1016_j_aqrep_2024_101939
crossref_primary_10_1002_ece3_70953
crossref_primary_10_1021_acsbiomaterials_1c00693
crossref_primary_10_1155_2016_5986519
crossref_primary_10_1016_j_margen_2015_01_009
crossref_primary_10_1007_s10750_018_3684_y
crossref_primary_10_1371_journal_pone_0021238
crossref_primary_10_1186_s12864_017_4161_0
crossref_primary_10_1080_09712119_2019_1624261
crossref_primary_10_3389_fmars_2022_984989
crossref_primary_10_1016_j_aquaculture_2020_735719
crossref_primary_10_1139_cjz_2012_0333
crossref_primary_10_1016_j_aqrep_2024_102357
crossref_primary_10_1038_srep45754
crossref_primary_10_1002_cbic_200700553
crossref_primary_10_1186_s12864_022_08575_9
Cites_doi 10.1073/pnas.81.6.1684
10.1146/annurev.arplant.49.1.697
10.1007/s10126-005-6029-6
10.1073/pnas.82.22.7585
10.1021/ja9819108
10.1111/j.1742-4658.2005.04899.x
10.1006/bbrc.2000.2274
10.1007/s10126-002-0048-3
10.1016/S0021-9258(18)68733-2
10.1042/bj2530877
10.1007/s00425-005-1558-9
10.1002/bip.10536
10.1006/bbrc.2001.5170
10.1016/j.msec.2005.01.003
10.1038/381056a0
10.1016/S0076-6879(83)91042-X
10.1074/jbc.M412680200
10.1074/jbc.M003006200
10.1002/ceat.200500354
10.1016/S0014-5793(99)01387-3
10.1016/j.crpv.2004.07.009
10.1073/pnas.0508480102
10.1126/science.271.5245.67
10.1128/IAI.58.6.1489-1495.1990
10.1016/j.jsb.2005.09.009
10.1016/j.cbpc.2004.03.012
ContentType Journal Article
Copyright 2007
Copyright_xml – notice: 2007
DBID AAYXX
CITATION
CGR
CUY
CVF
ECM
EIF
NPM
7X8
DOI 10.1016/j.bbagen.2007.06.018
DatabaseName CrossRef
Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
MEDLINE - Academic
DatabaseTitle CrossRef
MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
MEDLINE - Academic
DatabaseTitleList MEDLINE - Academic
MEDLINE

Database_xml – sequence: 1
  dbid: NPM
  name: PubMed
  url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed
  sourceTypes: Index Database
– sequence: 2
  dbid: EIF
  name: MEDLINE
  url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search
  sourceTypes: Index Database
DeliveryMethod fulltext_linktorsrc
Discipline Chemistry
Biology
EISSN 1872-8006
EndPage 1344
ExternalDocumentID 17692465
10_1016_j_bbagen_2007_06_018
S0304416507001298
Genre Research Support, Non-U.S. Gov't
Journal Article
GroupedDBID ---
--K
--M
.~1
0R~
1B1
1RT
1~.
1~5
23N
3O-
4.4
457
4G.
53G
5GY
5RE
5VS
7-5
71M
8P~
9JM
AACTN
AAEDT
AAEDW
AAIAV
AAIKJ
AAKOC
AALRI
AAOAW
AAQFI
AAQXK
AAXUO
ABEFU
ABFNM
ABGSF
ABMAC
ABUDA
ABXDB
ABYKQ
ACDAQ
ACIUM
ACRLP
ADBBV
ADEZE
ADMUD
ADUVX
AEBSH
AEHWI
AEKER
AFKWA
AFTJW
AFXIZ
AGHFR
AGRDE
AGUBO
AGYEJ
AHHHB
AIEXJ
AIKHN
AITUG
AJBFU
AJOXV
ALMA_UNASSIGNED_HOLDINGS
AMFUW
AMRAJ
ASPBG
AVWKF
AXJTR
AZFZN
BKOJK
BLXMC
CS3
DOVZS
EBS
EFJIC
EFLBG
EJD
EO8
EO9
EP2
EP3
FDB
FEDTE
FGOYB
FIRID
FNPLU
FYGXN
G-2
G-Q
GBLVA
HLW
HVGLF
HZ~
IHE
J1W
KOM
LX3
M41
MO0
N9A
O-L
O9-
OAUVE
OHT
OZT
P-8
P-9
PC.
Q38
R2-
ROL
RPZ
SBG
SCC
SDF
SDG
SDP
SES
SEW
SPCBC
SSU
SSZ
T5K
UQL
WH7
WUQ
XJT
XPP
~G-
AAHBH
AATTM
AAXKI
AAYWO
AAYXX
ABWVN
ACRPL
ACVFH
ADCNI
ADNMO
AEIPS
AEUPX
AFJKZ
AFPUW
AGCQF
AGQPQ
AGRNS
AIGII
AIIUN
AKBMS
AKRWK
AKYEP
ANKPU
APXCP
BNPGV
CITATION
SSH
-~X
.55
.GJ
AAYJJ
ABJNI
AFFNX
AI.
CGR
CUY
CVF
ECM
EIF
F5P
H~9
K-O
MVM
NPM
RIG
TWZ
UHS
VH1
X7M
Y6R
YYP
ZE2
ZGI
~KM
7X8
ID FETCH-LOGICAL-c426t-31ccbaf6c9b97c73308b7c33a25a8aa9b69356581af91357aa36483392738fc03
IEDL.DBID .~1
ISSN 0304-4165
0006-3002
IngestDate Fri Jul 11 08:14:17 EDT 2025
Mon Jul 21 05:42:47 EDT 2025
Tue Jul 01 00:21:53 EDT 2025
Thu Apr 24 23:07:34 EDT 2025
Fri Feb 23 02:32:37 EST 2024
IsPeerReviewed true
IsScholarly true
Issue 9
Keywords Biomineralization
Pearl oyster
Calmodulin-like protein
Organic layer
Pinctada fucata
Language English
License https://www.elsevier.com/tdm/userlicense/1.0
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c426t-31ccbaf6c9b97c73308b7c33a25a8aa9b69356581af91357aa36483392738fc03
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
PMID 17692465
PQID 68181575
PQPubID 23479
PageCount 7
ParticipantIDs proquest_miscellaneous_68181575
pubmed_primary_17692465
crossref_citationtrail_10_1016_j_bbagen_2007_06_018
crossref_primary_10_1016_j_bbagen_2007_06_018
elsevier_sciencedirect_doi_10_1016_j_bbagen_2007_06_018
ProviderPackageCode CITATION
AAYXX
PublicationCentury 2000
PublicationDate 2007-09-01
PublicationDateYYYYMMDD 2007-09-01
PublicationDate_xml – month: 09
  year: 2007
  text: 2007-09-01
  day: 01
PublicationDecade 2000
PublicationPlace Netherlands
PublicationPlace_xml – name: Netherlands
PublicationTitle Biochimica et biophysica acta
PublicationTitleAlternate Biochim Biophys Acta
PublicationYear 2007
Publisher Elsevier B.V
Publisher_xml – name: Elsevier B.V
References Sun, Blair, Peng, Zaidi, Adebanjo, Wu, Wu, Iqbal, Epstein, Abe, Moonga, Zaidi (bib15) 2005; 102
Masure, Oldenburg, Donovan, Shattuck, Storm (bib20) 1988; 263
Nelson, Tredgett, Sheehan, Thornton, Notman, Govan (bib24) 1990; 58
Falini, Albeck, Weiner, Addadi (bib3) 1996; 271
Zayzafoon, Fulzele, McDonald (bib16) 2005; 280
Marin, Luquet (bib7) 2005; 25
Nudelman, Gotliv, Addadi, Weiner (bib14) 2006; 153
Li, Xie, Zhang, Zhang, Gu, Zhang (bib8) 2004; 138
Li, Xie, Ma, Zhang (bib9) 2005; 272
Zielinski (bib17) 1998; 49
Belcher, Wu, Christensen, Hansma, Stucky, Morse (bib26) 1996; 381
Samata (bib25) 1999; 462
Zhang, Zhang (bib5) 2006; 8
Marin, Luquet (bib4) 2004; 3
Bhown, Bennett (bib12) 1983; 91
Xu, Yao, Aksay, Groves (bib13) 1998; 120
Michenfelder, Fu, Lawrence, Weaver, Wustman, Taranto, Evans, Morse (bib21) 2003; 70
Billingsley, Pennypacker, Hoover, Brigati, Kincaid (bib10) 1985; 82
Matsushiro, Miyashita, Miyamoto, Morimoto, Tonomura, Tanaka, Sato (bib22) 2003; 5
Dandeu, Humbert, Carteret, Muhr, Plasari, Bossoutrot (bib2) 2006; 29
Weiss, Gohring, Fritz, Mann (bib27) 2001; 285
Crocker, Dawson, Barton, MacNeil (bib19) 1988; 253
Marin, Corstjens, de Gaulejac, de Vrind-De Jong, Westbroek (bib6) 2000; 275
Kono, Hayashi, Samata (bib23) 2000; 269
Mann (bib1) 2001
Mao, Hou, Ding, Cui, Sun (bib18) 2005; 222
Jahn, Schiebler, Greengard (bib11) 1984; 81
Bhown (10.1016/j.bbagen.2007.06.018_bib12) 1983; 91
Dandeu (10.1016/j.bbagen.2007.06.018_bib2) 2006; 29
Xu (10.1016/j.bbagen.2007.06.018_bib13) 1998; 120
Zielinski (10.1016/j.bbagen.2007.06.018_bib17) 1998; 49
Mann (10.1016/j.bbagen.2007.06.018_bib1) 2001
Li (10.1016/j.bbagen.2007.06.018_bib8) 2004; 138
Billingsley (10.1016/j.bbagen.2007.06.018_bib10) 1985; 82
Sun (10.1016/j.bbagen.2007.06.018_bib15) 2005; 102
Kono (10.1016/j.bbagen.2007.06.018_bib23) 2000; 269
Marin (10.1016/j.bbagen.2007.06.018_bib4) 2004; 3
Crocker (10.1016/j.bbagen.2007.06.018_bib19) 1988; 253
Mao (10.1016/j.bbagen.2007.06.018_bib18) 2005; 222
Samata (10.1016/j.bbagen.2007.06.018_bib25) 1999; 462
Zayzafoon (10.1016/j.bbagen.2007.06.018_bib16) 2005; 280
Nudelman (10.1016/j.bbagen.2007.06.018_bib14) 2006; 153
Jahn (10.1016/j.bbagen.2007.06.018_bib11) 1984; 81
Weiss (10.1016/j.bbagen.2007.06.018_bib27) 2001; 285
Nelson (10.1016/j.bbagen.2007.06.018_bib24) 1990; 58
Falini (10.1016/j.bbagen.2007.06.018_bib3) 1996; 271
Masure (10.1016/j.bbagen.2007.06.018_bib20) 1988; 263
Zhang (10.1016/j.bbagen.2007.06.018_bib5) 2006; 8
Li (10.1016/j.bbagen.2007.06.018_bib9) 2005; 272
Marin (10.1016/j.bbagen.2007.06.018_bib7) 2005; 25
Matsushiro (10.1016/j.bbagen.2007.06.018_bib22) 2003; 5
Michenfelder (10.1016/j.bbagen.2007.06.018_bib21) 2003; 70
Belcher (10.1016/j.bbagen.2007.06.018_bib26) 1996; 381
Marin (10.1016/j.bbagen.2007.06.018_bib6) 2000; 275
References_xml – volume: 271
  start-page: 67
  year: 1996
  end-page: 69
  ident: bib3
  article-title: Control of aragonite or calcite polymorphism by mollusk shell macromolecules
  publication-title: Science
– volume: 462
  start-page: 225
  year: 1999
  end-page: 229
  ident: bib25
  article-title: A new matrix protein family related to the nacreous layer formation of
  publication-title: FEBS Lett.
– volume: 91
  start-page: 450
  year: 1983
  end-page: 455
  ident: bib12
  article-title: High-sensitivity sequence analysis of protein recovered from sodium dodecyl sulfate gel
  publication-title: Methods Enzymol.
– volume: 25
  start-page: 105
  year: 2005
  end-page: 111
  ident: bib7
  article-title: Molluscan biomineralization: the proteinaceous shell constituents of
  publication-title: Mater. Sci. Eng., C, Biomim. Mater., Sens. Syst.
– volume: 138
  start-page: 235
  year: 2004
  end-page: 243
  ident: bib8
  article-title: Cloning and expression of a pivotal calcium metabolism regulator: calmodulin involved in shell formation from pearl oyster (
  publication-title: Comp. Biochem. Physiol., Part B Biochem. Mol. Biol.
– volume: 280
  start-page: 7049
  year: 2005
  end-page: 7059
  ident: bib16
  article-title: Calmodulin and calmodulin-dependent kinase IIalpha regulate osteoblast differentiation by controlling c-
  publication-title: J. Biol. Chem.
– volume: 29
  start-page: 221
  year: 2006
  end-page: 225
  ident: bib2
  article-title: Raman spectroscopy — a powerful tool for the quantitative determination of the composition of polymorph mixtures: application to CaCO
  publication-title: Chem. Eng. Technol.
– volume: 269
  start-page: 213
  year: 2000
  end-page: 218
  ident: bib23
  article-title: Molecular mechanism of the nacreous layer formation in
  publication-title: Biochem. Biophys. Res. Commun.
– volume: 120
  start-page: 11977
  year: 1998
  end-page: 11985
  ident: bib13
  article-title: Biomimetic synthesis of macroscopic-scale calcium carbonate thin films. Evidence for a multistep assembly process
  publication-title: J. Am. Chem. Soc.
– volume: 253
  start-page: 877
  year: 1988
  end-page: 884
  ident: bib19
  article-title: An extracellular role for calmodulin-like activity in cell proliferation
  publication-title: Biochem. J.
– year: 2001
  ident: bib1
  article-title: Biomineralization. Principles and concepts in bioinorganic materials chemistry
– volume: 8
  start-page: 572
  year: 2006
  end-page: 586
  ident: bib5
  article-title: Matrix proteins in the outer shells of molluscs
  publication-title: Mar. Biotechnol.
– volume: 263
  start-page: 6933
  year: 1988
  end-page: 6940
  ident: bib20
  article-title: The interaction of Ca
  publication-title: J. Biol. Chem.
– volume: 70
  start-page: 522
  year: 2003
  end-page: 533
  ident: bib21
  article-title: Characterization of two molluscan crystal-modulating biomineralization proteins and identification of putative mineral binding domains
  publication-title: Biopolymers
– volume: 82
  start-page: 7585
  year: 1985
  end-page: 7589
  ident: bib10
  article-title: A rapid and sensitive method for detection and quantification of calcineurin and calmodulin-binding proteins using biotinylated calmodulin
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
– volume: 285
  start-page: 244
  year: 2001
  end-page: 249
  ident: bib27
  article-title: Perlustrin, a
  publication-title: Biochem. Biophys. Res. Commun.
– volume: 275
  start-page: 20667
  year: 2000
  end-page: 20675
  ident: bib6
  article-title: Mucins and molluscan calcification. Molecular characterization of mucoperlin, a novel mucin-like protein from the nacreous shell layer of the fan mussel
  publication-title: J. Biol. Chem.
– volume: 81
  start-page: 1684
  year: 1984
  end-page: 1687
  ident: bib11
  article-title: A quantitative dot-immunobinding assay for proteins using nitrocellulose membrane filters
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
– volume: 3
  start-page: 469
  year: 2004
  end-page: 492
  ident: bib4
  article-title: Molluscan shell proteins
  publication-title: C. R. Palevol.
– volume: 5
  start-page: 37
  year: 2003
  end-page: 44
  ident: bib22
  article-title: Presence of protein complex is prerequisite for aragonite crystallization in the nacreous layer
  publication-title: Mar. Biotechnol. (NY)
– volume: 102
  start-page: 17130
  year: 2005
  end-page: 17135
  ident: bib15
  article-title: Calcineurin regulates bone formation by the osteoblast
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
– volume: 153
  start-page: 176
  year: 2006
  end-page: 187
  ident: bib14
  article-title: Mollusk shell formation: mapping the distribution of organic matrix components underlying a single aragonitic tablet in nacre
  publication-title: J. Struct. Biol.
– volume: 58
  start-page: 1489
  year: 1990
  end-page: 1495
  ident: bib24
  article-title: Mucinophilic and chemotactic properties of
  publication-title: Infect. Immun.
– volume: 49
  start-page: 697
  year: 1998
  end-page: 725
  ident: bib17
  article-title: Calmodulin and calmodulin-binding proteins in plants
  publication-title: Annu. Rev. Plant Physiol. Plant Mol. Biol.
– volume: 381
  start-page: 56
  year: 1996
  end-page: 58
  ident: bib26
  article-title: Control of crystal phase switching and orientation by soluble mollusc-shell proteins
  publication-title: Nature
– volume: 272
  start-page: 4899
  year: 2005
  end-page: 4910
  ident: bib9
  article-title: cDNA cloning and characterization of a novel calmodulin-like protein from pearl oyster
  publication-title: FEBS J.
– volume: 222
  start-page: 428
  year: 2005
  end-page: 437
  ident: bib18
  article-title: Characterization of a cDNA coding for an extracellular calmodulin-binding protein from suspension-cultured cells of
  publication-title: Planta
– volume: 81
  start-page: 1684
  year: 1984
  ident: 10.1016/j.bbagen.2007.06.018_bib11
  article-title: A quantitative dot-immunobinding assay for proteins using nitrocellulose membrane filters
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.81.6.1684
– volume: 49
  start-page: 697
  year: 1998
  ident: 10.1016/j.bbagen.2007.06.018_bib17
  article-title: Calmodulin and calmodulin-binding proteins in plants
  publication-title: Annu. Rev. Plant Physiol. Plant Mol. Biol.
  doi: 10.1146/annurev.arplant.49.1.697
– volume: 8
  start-page: 572
  year: 2006
  ident: 10.1016/j.bbagen.2007.06.018_bib5
  article-title: Matrix proteins in the outer shells of molluscs
  publication-title: Mar. Biotechnol.
  doi: 10.1007/s10126-005-6029-6
– volume: 82
  start-page: 7585
  year: 1985
  ident: 10.1016/j.bbagen.2007.06.018_bib10
  article-title: A rapid and sensitive method for detection and quantification of calcineurin and calmodulin-binding proteins using biotinylated calmodulin
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.82.22.7585
– volume: 120
  start-page: 11977
  year: 1998
  ident: 10.1016/j.bbagen.2007.06.018_bib13
  article-title: Biomimetic synthesis of macroscopic-scale calcium carbonate thin films. Evidence for a multistep assembly process
  publication-title: J. Am. Chem. Soc.
  doi: 10.1021/ja9819108
– volume: 272
  start-page: 4899
  year: 2005
  ident: 10.1016/j.bbagen.2007.06.018_bib9
  article-title: cDNA cloning and characterization of a novel calmodulin-like protein from pearl oyster Pinctada fucata
  publication-title: FEBS J.
  doi: 10.1111/j.1742-4658.2005.04899.x
– volume: 269
  start-page: 213
  year: 2000
  ident: 10.1016/j.bbagen.2007.06.018_bib23
  article-title: Molecular mechanism of the nacreous layer formation in Pinctada maxima
  publication-title: Biochem. Biophys. Res. Commun.
  doi: 10.1006/bbrc.2000.2274
– volume: 5
  start-page: 37
  year: 2003
  ident: 10.1016/j.bbagen.2007.06.018_bib22
  article-title: Presence of protein complex is prerequisite for aragonite crystallization in the nacreous layer
  publication-title: Mar. Biotechnol. (NY)
  doi: 10.1007/s10126-002-0048-3
– volume: 263
  start-page: 6933
  year: 1988
  ident: 10.1016/j.bbagen.2007.06.018_bib20
  article-title: The interaction of Ca2+ with the calmodulin-sensitive adenylate cyclase from Bordetella pertussis
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(18)68733-2
– volume: 253
  start-page: 877
  year: 1988
  ident: 10.1016/j.bbagen.2007.06.018_bib19
  article-title: An extracellular role for calmodulin-like activity in cell proliferation
  publication-title: Biochem. J.
  doi: 10.1042/bj2530877
– volume: 222
  start-page: 428
  year: 2005
  ident: 10.1016/j.bbagen.2007.06.018_bib18
  article-title: Characterization of a cDNA coding for an extracellular calmodulin-binding protein from suspension-cultured cells of Angelica dahurica
  publication-title: Planta
  doi: 10.1007/s00425-005-1558-9
– volume: 70
  start-page: 522
  year: 2003
  ident: 10.1016/j.bbagen.2007.06.018_bib21
  article-title: Characterization of two molluscan crystal-modulating biomineralization proteins and identification of putative mineral binding domains
  publication-title: Biopolymers
  doi: 10.1002/bip.10536
– volume: 285
  start-page: 244
  year: 2001
  ident: 10.1016/j.bbagen.2007.06.018_bib27
  article-title: Perlustrin, a Haliotis laevigata (abalone) nacre protein, is homologous to the insulin-like growth factor binding protein N-terminal module of vertebrates
  publication-title: Biochem. Biophys. Res. Commun.
  doi: 10.1006/bbrc.2001.5170
– volume: 25
  start-page: 105
  year: 2005
  ident: 10.1016/j.bbagen.2007.06.018_bib7
  article-title: Molluscan biomineralization: the proteinaceous shell constituents of Pinna nobilis L.
  publication-title: Mater. Sci. Eng., C, Biomim. Mater., Sens. Syst.
  doi: 10.1016/j.msec.2005.01.003
– volume: 381
  start-page: 56
  year: 1996
  ident: 10.1016/j.bbagen.2007.06.018_bib26
  article-title: Control of crystal phase switching and orientation by soluble mollusc-shell proteins
  publication-title: Nature
  doi: 10.1038/381056a0
– volume: 91
  start-page: 450
  year: 1983
  ident: 10.1016/j.bbagen.2007.06.018_bib12
  article-title: High-sensitivity sequence analysis of protein recovered from sodium dodecyl sulfate gel
  publication-title: Methods Enzymol.
  doi: 10.1016/S0076-6879(83)91042-X
– volume: 280
  start-page: 7049
  year: 2005
  ident: 10.1016/j.bbagen.2007.06.018_bib16
  article-title: Calmodulin and calmodulin-dependent kinase IIalpha regulate osteoblast differentiation by controlling c-fos expression
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M412680200
– volume: 275
  start-page: 20667
  year: 2000
  ident: 10.1016/j.bbagen.2007.06.018_bib6
  article-title: Mucins and molluscan calcification. Molecular characterization of mucoperlin, a novel mucin-like protein from the nacreous shell layer of the fan mussel Pinna nobilis (Bivalvia, pteriomorphia)
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M003006200
– volume: 29
  start-page: 221
  year: 2006
  ident: 10.1016/j.bbagen.2007.06.018_bib2
  article-title: Raman spectroscopy — a powerful tool for the quantitative determination of the composition of polymorph mixtures: application to CaCO3 polymorph mixtures
  publication-title: Chem. Eng. Technol.
  doi: 10.1002/ceat.200500354
– volume: 462
  start-page: 225
  year: 1999
  ident: 10.1016/j.bbagen.2007.06.018_bib25
  article-title: A new matrix protein family related to the nacreous layer formation of Pinctada fucata
  publication-title: FEBS Lett.
  doi: 10.1016/S0014-5793(99)01387-3
– volume: 3
  start-page: 469
  year: 2004
  ident: 10.1016/j.bbagen.2007.06.018_bib4
  article-title: Molluscan shell proteins
  publication-title: C. R. Palevol.
  doi: 10.1016/j.crpv.2004.07.009
– volume: 102
  start-page: 17130
  year: 2005
  ident: 10.1016/j.bbagen.2007.06.018_bib15
  article-title: Calcineurin regulates bone formation by the osteoblast
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.0508480102
– year: 2001
  ident: 10.1016/j.bbagen.2007.06.018_bib1
– volume: 271
  start-page: 67
  year: 1996
  ident: 10.1016/j.bbagen.2007.06.018_bib3
  article-title: Control of aragonite or calcite polymorphism by mollusk shell macromolecules
  publication-title: Science
  doi: 10.1126/science.271.5245.67
– volume: 58
  start-page: 1489
  year: 1990
  ident: 10.1016/j.bbagen.2007.06.018_bib24
  article-title: Mucinophilic and chemotactic properties of Pseudomonas aeruginosa in relation to pulmonary colonization in cystic fibrosis
  publication-title: Infect. Immun.
  doi: 10.1128/IAI.58.6.1489-1495.1990
– volume: 153
  start-page: 176
  year: 2006
  ident: 10.1016/j.bbagen.2007.06.018_bib14
  article-title: Mollusk shell formation: mapping the distribution of organic matrix components underlying a single aragonitic tablet in nacre
  publication-title: J. Struct. Biol.
  doi: 10.1016/j.jsb.2005.09.009
– volume: 138
  start-page: 235
  year: 2004
  ident: 10.1016/j.bbagen.2007.06.018_bib8
  article-title: Cloning and expression of a pivotal calcium metabolism regulator: calmodulin involved in shell formation from pearl oyster (Pinctada fucata)
  publication-title: Comp. Biochem. Physiol., Part B Biochem. Mol. Biol.
  doi: 10.1016/j.cbpc.2004.03.012
SSID ssj0000595
ssj0025309
Score 2.090686
Snippet Calmodulin-like protein (CaLP) was believed to be involved in the shell formation of pearl oyster. However, no further study of this protein was ever...
SourceID proquest
pubmed
crossref
elsevier
SourceType Aggregation Database
Index Database
Enrichment Source
Publisher
StartPage 1338
SubjectTerms Animals
Biomineralization
Calcification, Physiologic - physiology
Calcium Carbonate - chemistry
Calcium Carbonate - metabolism
Calmodulin - physiology
Calmodulin-like protein
Immunohistochemistry
Organic layer
Pearl oyster
Pinctada
Pinctada fucata
Recombinant Proteins - isolation & purification
Recombinant Proteins - pharmacology
Title Biomineralization: Functions of calmodulin-like protein in the shell formation of pearl oyster
URI https://dx.doi.org/10.1016/j.bbagen.2007.06.018
https://www.ncbi.nlm.nih.gov/pubmed/17692465
https://www.proquest.com/docview/68181575
Volume 1770
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1LT-MwEB4hENq9IGAflKcPezVtceIHN1RRFarlsLtoOW1ku7EUKElF2wMXfjszTgJC2hXSSpESWbZiecaez_Y3MwDfJpTxyOeeo_HVPJEhcJ3qwL3qmdyjCfKBNorfr-ToOrm8SW9WYND6whCtsln76zU9rtZNSbcZze6sKLo_6VIP4QQCmniaQg6_SaJIy4-fXmkeCB_S-iYh4VS7dZ-LHC_ncNKWTSBDedyj1B9_N0__gp_RDA03YaPBj-ys7uIWrOTlNqzXGSUft-HDoE3g9gn-YOl9EaNKN86Wp2yIZixqGqsCQ_HcVxOiovNpcZezGLOhKBk-CAvZnDii7MW7kVrMcF5MWUXRnx8-w_Xw_NdgxJt0CtyjGV7gauu9s0F644zySoiedsoLYU9Sq601ThqB8E73bTB9kSprhUy0QAClhA6-J77AalmV-Q4wmxiNUMj5E4OfIbHOCmMnXsb4dWHSAdGOYuabWOOU8mKataSy26wee0qDqTLi1vV1B_hLq1kda-Od-qoVUPZGZzI0B--0PGrlmaFQ6I7Elnm1nGcSAUwfIWwHvtZifu2JkrhXlenuf_91Dz7WJ8PEUNuH1cXDMj9ASLNwh1FnD2Ht7GI8uqL3-Mfv8TO0VPcn
linkProvider Elsevier
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1LT9wwEB4BVUUviNLSLoWuD1zNPpz4wa1asdq2CxdA4lTL9sZS6G6y2seBC7-dsZOAkEBISDlElq1EHtvz2f5mPoDjSVA8cpmj6HwlTbj3VKbSUye6KnPogpwPG8XzCz66Tv7cpDcbMGhiYQKtsl77qzU9rtZ1Safuzc48zzuX4VIP4QQCmniaIjfhQ4LTN8gYnNw_8TwQP6TVVUJCQ_Umfi6SvKzFWVvUmQz5STdof7zsn17Dn9EPDXdhpwaQ5Ff1j59hIyv24GMlKXm3B9uDRsHtC_zD0lke00rX0ZanZIh-LA41UnqC9pmVk8BFp9P8f0Zi0oa8IPggLiTLQBIlj-GNocUcJ8aUlCH98-IrXA_PrgYjWuspUId-eIXLrXPWeO6UVcIJxrrSCseY6adGGqMsVwzxnewZr3osFcYwnkiGCEow6V2X7cNWURbZdyAmURKxkHV9ha8-MdYwZSaOxwR2ftIC1vSidnWy8aB5MdUNq-xWV30fdDCFDuS6nmwBfWw1r5JtvFFfNAbSzwaNRn_wRst2Y0-NRgmXJKbIyvVSc0QwPcSwLfhWmfnpTwTHzSpPD9791TZsj67Ox3r8--LvD_hUHRMHutohbK0W6-wI8c3K_ozj9wGc1PcS
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Biomineralization%3A+functions+of+calmodulin-like+protein+in+the+shell+formation+of+pearl+oyster&rft.jtitle=Biochimica+et+biophysica+acta&rft.au=Yan%2C+Zhenguang&rft.au=Fang%2C+Zi&rft.au=Ma%2C+Zhuojun&rft.au=Deng%2C+Jinye&rft.date=2007-09-01&rft.issn=0006-3002&rft.volume=1770&rft.issue=9&rft.spage=1338&rft_id=info:doi/10.1016%2Fj.bbagen.2007.06.018&rft_id=info%3Apmid%2F17692465&rft.externalDocID=17692465
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0304-4165&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0304-4165&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0304-4165&client=summon