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1 to 6 Chains of Type IV Collagen in Bovine Follicles1
a Department of Medicine, Flinders University of South Australia, Bedford Park, South Australia 5042, Australia
b Division of Animal Physiology, School of Biological Sciences, University of Nottingham, Sutton Bonington Campus, Loughborough LE12 5RD, United Kingdom
c Division of Immunology, Shigei Medical Research Institute, Okayama, 701–0202, Japan
d Department of Molecular Biology and Biochemistry, Okayama University Medical School, Okayama, 700–8558, Japan
During follicular development the proliferative and differentiated state of the epithelioid granulosa cells changes, and the movement of fluid across the follicular basal lamina enables the formation of an antrum. Type IV collagen is an important component of many basal laminae. Each molecule is composed of three chains; however, six different type IV collagen chains have been identified. It is not known which of these chains are present in the follicular basal lamina and whether the type IV collagen composition of the basal lamina changes during follicular development. Therefore, we immunolocalized each of the six chains in bovine ovaries using antibodies directed to the nonconserved non-collagenous (NC) domains. Additionally, dissected follicles were digested with collagenase to release the NC domains, and the NC1 domains were then detected by standard Western immunoblot methods. The follicular basal lamina of almost all primordial and preantral follicles was positive for all type IV collagen chains. Colocalization of type IV collagen and factor VIII-related antigen allowed for discrimination between the follicular and endothelial basal laminae. Type IV collagen 1, 2, 3, 4, and 5 chains were present within the follicular basal lamina of only a proportion of antral follicles (17 of 22, 20 of 21, 15 of 18, 14 of 28, and 12 of 23, respectively), and staining was less intense than in the preantral follicles. Staining for the 1 and 2 chains was diffusely distributed throughout the theca in regions not associated with recognized basal laminae. The specificity of this immunostaining for 1 and 2 chains of type IV collagen was confirmed by Western immunoblots. As well as being detected in the basal lamina of approximately half of the antral follicles examined, type IV collagen 4 also colocalized with 3ß-hydroxysteroid dehydrogenase-immunopositive cells in the theca interna. Type IV collagen 6 was detected in the basal lamina of only one of the 16 antral follicles examined. Thus, the follicular basal lamina changes in composition during follicular development, with immunostaining levels being reduced for all type IV collagen chains and immunoreactivity for type IV collagen 6 being lost as follicle size increases. Additionally, immunoreactivity for 1 and 2 appears in the extracellular matrix of the theca as it develops.
2 Correspondence. FAX: 61 8 82045450; ray.rodgers{at}Flinders.edu.au
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