Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P39060 (endostatin)
 2,284 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Laminin, collagen IV, collagen XVIII, agrin, and nidogen are major protein constituents of the chick retinal basal lamina. To determine their sites of synthesis during de novo basal lamina assembly in vivo, we localized their mRNA expression in the eye during maximum expansion of the retina between embryonic day (E) 2.5 and E6. Our in situ hybridization studies showed that the expression pattern of every basal lamina protein mRNA in the developing eye is unique. Collagen IV and perlecan originate predominantly from the lens epithelium, whereas collagen XVIII, nidogen, and the laminin gamma 1 and beta1 chains are synthesized mainly by the ciliary body. Agrin, collagen XVIII, collagen IV, and laminin gamma 1 also originate from cells of the optic disc. The only basal lamina protein that is synthesized by the neural retina throughout development is agrin with ganglion cells as its main source. Some of the mRNAs have short, transient expressions in the retina, most notably that of collagen IV and laminin gamma 1, both of which appear in the ventral retina between E4 and E5. That most retinal basal lamina proteins originate from extraretinal tissues infers that the basal lamina proteins have to be shed from the lens, optic disc, and ciliary body into the vitreous body. The assembly of the retinal basal lamina then occurs by the binding of these proteins by cellular receptor proteins on the vitreal endfeet of the retinal neuroepithelial cells.
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PMID:Expression of basal lamina protein mRNAs in the early embryonic chick eye. 1198 20

Basement membranes lie at the epithelial-mesenchymal interface of most tissues. These thin layers of highly specialized extracellular matrix vary in composition in different tissues and also over the course of tissue morphogenesis. Heparan sulfate proteoglycans, which were originally identified in basement membranes, interact with extracellular matrix proteins, growth factors and cell receptors, and influence cellular signaling. Members of this family in the human placenta and decidua that act principally in linking to collagen IV and laminin networks include perlecan, agrin, and collagen XVIII, each of which have characteristic locations. Perlecan is widely expressed in trophoblasts, the villous and endothelial basement membranes, villous stroma, and decidua, whereas collagen XVIII is not expressed in trophoblasts. Agrin expression is quite limited, occurring only in the decidua and villous stroma. Pathological conditions may alter the expression and structure of the covalently attached glycosaminoglycan chains of these molecules in the placenta. Such changes may result in remodeling of the basement membrane during placental development with consequent adverse effects, as seen for example in gestational diabetes and other diseases or experimental models.
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PMID:Heparan sulfate proteoglycans in the basement membranes of the human placenta and decidua. 1829 21