Kallikreins on Steroids: Structure, Function, and Hormonal Regulation of Prostate-Specific Antigen and the Extended Kallikrein Locus

The 15 members of the kallikrein-related serine peptidase (KLK) family have diverse tissue-specific expression profiles and putative proteolytic functions. The kallikrein family is also emerging as a rich source of disease biomarkers with KLK3, commonly known as prostate-specific antigen, being the...

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Published inEndocrine reviews Vol. 31; no. 4; pp. 407 - 446
Main Authors Lawrence, Mitchell G, Lai, John, Clements, Judith A
Format Journal Article
LanguageEnglish
Published Bethesda, MD Endocrine Society 01.08.2010
Oxford University Press
Copyright by The Endocrine Society
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Abstract The 15 members of the kallikrein-related serine peptidase (KLK) family have diverse tissue-specific expression profiles and putative proteolytic functions. The kallikrein family is also emerging as a rich source of disease biomarkers with KLK3, commonly known as prostate-specific antigen, being the current serum biomarker for prostate cancer. The kallikrein locus is also notable because it is extraordinarily responsive to steroids and other hormones. Indeed, at least 14 functional hormone response elements have been identified in the kallikrein locus. A more comprehensive understanding of the transcriptional regulation of kallikreins may help the field make more informed hypotheses about the physiological functions of kallikreins and their effectiveness as biomarkers. In this review, we describe the organization of the kallikrein locus and the structure of kallikrein genes and proteins. We also focus on the transcriptional regulation of kallikreins by androgens, progestins, glucocorticoids, mineralocorticoids, estrogens, and other hormones in animal models and human prostate, breast, and reproductive tract tissues. The interaction of the androgen receptor with androgen response elements in the promoter and enhancer of KLK2 and KLK3 is also summarized in detail. There is evidence that all kallikreins are regulated by multiple nuclear receptors. Yet, apart from KLK2 and KLK3, it is not clear whether all kallikreins are direct transcriptional targets. Therefore, we argue that gaining more detailed information about the mechanisms that regulate kallikrein expression should be a priority of future studies and that the kallikrein locus will continue to be an important model in the era of genome-wide analyses.
AbstractList The 15 members of the kallikrein-related serine peptidase (KLK) family have diverse tissue-specific expression profiles and putative proteolytic functions. The kallikrein family is also emerging as a rich source of disease biomarkers with KLK3, commonly known as prostate-specific antigen, being the current serum biomarker for prostate cancer. The kallikrein locus is also notable because it is extraordinarily responsive to steroids and other hormones. Indeed, at least 14 functional hormone response elements have been identified in the kallikrein locus. A more comprehensive understanding of the transcriptional regulation of kallikreins may help the field make more informed hypotheses about the physiological functions of kallikreins and their effectiveness as biomarkers. In this review, we describe the organization of the kallikrein locus and the structure of kallikrein genes and proteins. We also focus on the transcriptional regulation of kallikreins by androgens, progestins, glucocorticoids, mineralocorticoids, estrogens, and other hormones in animal models and human prostate, breast, and reproductive tract tissues. The interaction of the androgen receptor with androgen response elements in the promoter and enhancer of KLK2 and KLK3 is also summarized in detail. There is evidence that all kallikreins are regulated by multiple nuclear receptors. Yet, apart from KLK2 and KLK3, it is not clear whether all kallikreins are direct transcriptional targets. Therefore, we argue that gaining more detailed information about the mechanisms that regulate kallikrein expression should be a priority of future studies and that the kallikrein locus will continue to be an important model in the era of genome-wide analyses. Kallikrein-related serine peptidases have diverse tissue- and disease-specific expression profiles and proteolytic functions. A prominent member of the kallikrein family, prostate-specific antigen, is the current serum biomarker for prostate cancer and is commonly used as a model target gene to study the actions of the androgen receptor. This review focuses on the regulation of kallikrein gene expression by steroid hormone receptors and other nuclear receptors as well as the structure, evolution and proteolytic functions of the kallikrein family.
The 15 members of the kallikrein-related serine peptidase (KLK) family have diverse tissue-specific expression profiles and putative proteolytic functions. The kallikrein family is also emerging as a rich source of disease biomarkers with KLK3, commonly known as prostate-specific antigen, being the current serum biomarker for prostate cancer. The kallikrein locus is also notable because it is extraordinarily responsive to steroids and other hormones. Indeed, at least 14 functional hormone response elements have been identified in the kallikrein locus. A more comprehensive understanding of the transcriptional regulation of kallikreins may help the field make more informed hypotheses about the physiological functions of kallikreins and their effectiveness as biomarkers. In this review, we describe the organization of the kallikrein locus and the structure of kallikrein genes and proteins. We also focus on the transcriptional regulation of kallikreins by androgens, progestins, glucocorticoids, mineralocorticoids, estrogens, and other hormones in animal models and human prostate, breast, and reproductive tract tissues. The interaction of the androgen receptor with androgen response elements in the promoter and enhancer of KLK2 and KLK3 is also summarized in detail. There is evidence that all kallikreins are regulated by multiple nuclear receptors. Yet, apart from KLK2 and KLK3, it is not clear whether all kallikreins are direct transcriptional targets. Therefore, we argue that gaining more detailed information about the mechanisms that regulate kallikrein expression should be a priority of future studies and that the kallikrein locus will continue to be an important model in the era of genome-wide analyses.
Author Lawrence, Mitchell G
Clements, Judith A
Lai, John
AuthorAffiliation Australian Prostate Cancer Research Centre-Queensland and the Institute of Health and Biomedical Innovation, Queensland University of Technology, Brisbane 4059, Australia; and the Australian Prostate Cancer BioResource, Adelaide 5000, Australia
AuthorAffiliation_xml – name: Australian Prostate Cancer Research Centre-Queensland and the Institute of Health and Biomedical Innovation, Queensland University of Technology, Brisbane 4059, Australia; and the Australian Prostate Cancer BioResource, Adelaide 5000, Australia
Author_xml – sequence: 1
  givenname: Mitchell G
  surname: Lawrence
  fullname: Lawrence, Mitchell G
– sequence: 2
  givenname: John
  surname: Lai
  fullname: Lai, John
– sequence: 3
  givenname: Judith A
  surname: Clements
  fullname: Clements, Judith A
BackLink http://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=23277085$$DView record in Pascal Francis
https://www.ncbi.nlm.nih.gov/pubmed/20103546$$D View this record in MEDLINE/PubMed
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Snippet The 15 members of the kallikrein-related serine peptidase (KLK) family have diverse tissue-specific expression profiles and putative proteolytic functions. The...
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SubjectTerms Androgen receptors
Androgens
Androgens - pharmacology
Animal models
Animals
Antigens
Biological and medical sciences
Biomarkers
Biomarkers, Tumor - blood
Breast - chemistry
Chromosomes, Human, Pair 19
Estrogens
Estrogens - pharmacology
Evolution, Molecular
Female
Functional morphology
Functionals
Fundamental and applied biological sciences. Psychology
Gene Expression Regulation - drug effects
Gene regulation
Genetic Loci - genetics
Glucocorticoids
Glucocorticoids - pharmacology
Hormones
Hormones - pharmacology
Humans
Kallikrein gene
Kallikreins
Kallikreins - chemistry
Kallikreins - genetics
Kallikreins - physiology
Loci
Male
Mineralocorticoids
Models, Molecular
Molecular Structure
Nuclear receptors
Polymorphism, Genetic
Progestin
Progestins - pharmacology
Promoter Regions, Genetic - genetics
Prostate
Prostate - chemistry
Prostate cancer
Prostate-specific antigen
Prostate-Specific Antigen - chemistry
Prostate-Specific Antigen - genetics
Prostate-Specific Antigen - physiology
Prostatic Neoplasms - blood
Proteolysis
Receptors
Regulatory sequences
Reproductive system
Serine peptidase
Steroid hormones
Steroids
Structure-function relationships
Transcription
Vertebrates: endocrinology
Title Kallikreins on Steroids: Structure, Function, and Hormonal Regulation of Prostate-Specific Antigen and the Extended Kallikrein Locus
URI http://dx.doi.org/10.1210/er.2009-0034
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https://www.ncbi.nlm.nih.gov/pubmed/20103546
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Volume 31
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