Distribution of Fibronectin and Collagen during Mouse Limb and Palate Development

• Published in: Differentiation (London) Vol. 18; no. 1; pp. 141 - 149
• Main Authors: SILVER, MICHAEL H., FOIDART, JEAN-MICHEL, PRATT, ROBERT M.
• Format: Journal Article Web Resource
• Language: English
• Published: Oxford, UK Elsevier B.V 01.01.1981; Blackwell Publishing Ltd; Blackwell Publishing
• Subjects: Animals; Biochemistry, biophysics & molecular biology; Biochimie, biophysique & biologie moléculaire; Collagen - metabolism; Female; Fibronectins - metabolism; Fluorescent Antibody Technique; Forelimb - embryology; Forelimb - metabolism; Germ Layers - metabolism; Histocytochemistry; Life sciences; Mice; Palate - embryology; Palate - metabolism; Pregnancy; Sciences du vivant
• ISSN: 0301-4681; 1432-0436; 1432-0436
• DOI: 10.1111/j.1432-0436.1981.tb01115.x

Indirect immunofluorescence has been used to study the distribution of fibronectin and collagen types I, II, and III in the developing primary and secondary palatal processes and forelimb buds of the Swiss Webster (NIH) mouse. In the palatal processes fibronectin and types I and III collagen are distributed throughout the mesenchyme. Fibronectin is present in the basement membrane, while types I and III collagen are localized in a linear, discontinuous fashion beneath the basement membrane. Fibronectin is not observed in the epithelium, including the presumptive fusion areas. In the forelimb bud these components show a similar distribution prior to chondrogenesis (early day 11). When chondrogenesis commences (late day 11 or early day 12) fibronectin and, to a lesser degree, types I and III collagen are apparently concentrated in the core mesenchyme, suggesting that fibronectin has a role in initiating chondrogenesis, perhaps by increasing cellular aggregation. Type II collagen is observed only in chondrogenic regions. The codistribution of fibronectin and types I and III collagen supports in vitro studies which indicate that cells use fibronectin to bind to collagen in the matrix. The developing chondrogenic regions appear to lose fibronectin gradually, concomitant with the appearance of type II collagen, suggesting that fibronectin is not involved in the maintenance of functional chondrocytes in their matrices.