Isolation and native characterization of cysteine-rich collagens from bovine placental tissues and uterus and their relationship to types IV and V collagens

Background: ␣1(V) is an extensively modified collagen chain important in disease. Results: Comprehensive mapping of ␣1(V) post-translational modifications reveals unexpectedly large numbers of X-position hydroxyprolines in Gly-X-Y amino acid triplets. Conclusion:The unexpected abundance of X-position hydroxyprolines suggests a mechanism for differential modification of collagen properties. Significance: Positions, numbers, and occupancy of modified sites can provide insights into ␣1(V) biological properties.

Section: Comparison Of the Col1 Ptms Of Bovine Placental ␣1(v) And Husupporting

confidence: 84%

Section: Comparison Of the Col1 Ptms Of Bovine Placental ␣1(v) And Husupporting

confidence: 81%

Comprehensive Mass Spectrometric Mapping of the Hydroxylated Amino Acid residues of the α1(V) Collagen Chain

Yang

Park

Davis

et al. 2012

“…Expression of α3(V) polypeptide has also been demonstrated by biochemical methods in placenta (14) and uterus (15). In situ hybridization analysis of 15.5 dpc mouse embryos, on the other hand, failed to detect putative collagen α3(V) mRNA expression in heart or lung.…”

Section: Discussionmentioning

confidence: 99%

Schwann Cells Synthesize Type V Collagen That Contains a Novel α4 Chain

Chernousov

Rothblum

Tyler

et al. 2000

SUMMARYPreviously, we reported the isolation of a heparan sulfate-binding collagenous protein, p200, that is expressed by Schwann cells in developing peripheral nerves (J. Biol. Chem. 271:13844-13853, 1996; J. Neurosci. Res. 56:284-294, 1999). Here we report the cloning of p200 cDNA from a Schwann cell cDNA library. The deduced amino acid sequence identifies p200 as a novel member of the collagen type V gene family. This polypeptide, which we have named α4 type V collagen, contains an uninterrupted Gly-X-X collagen domain of 1011 amino acids that shows 82% sequence identity to human α3(V) collagen and 71% identity to rat α1(V) collagen. α4(V) is secreted by Schwann cells as a collagen heterotrimer that also contains α1(V) chains. α4(V)-containing collagen molecules synthesized by Schwann cells retain their Nterminal non-collagenous domains. α4(V) mRNA was detected by reverse transcriptase-linked PCR amplification in neonatal and adult brain and neonatal peripheral nerve. α4(V) mRNA and protein were not detected in most other tissues, including placenta and heart, which are known to contain α3(V). This pattern of α4(V) expression contrasted with that of α1(V) mRNA and protein, which were ubiquitously expressed. The isolated α4(V) chain demonstrated an unusually high affinity for heparin. The restricted expression and unusual properties of α4(V)-containing collagen type V molecules suggest a unique and important role for these molecules in peripheral nerve development.

“…The ␣3(V) chain was also isolated from synovial membrane, gingival, skin (11), and uterus (54). In situ hybridization of mouse embryo detects ␣3(V) expression in the epimysial sheaths of developing muscles and within nascent ligaments adjacent to forming bones and in joints (16).…”

Section: Discussionmentioning

confidence: 99%

The Transcription Factor CCAAT-binding Factor CBF/NF-Y and Two Repressors Regulate the Core Promoter of the Human Pro-α3(V) Collagen Gene (COL5A3)

Nagato

Matsuo²,

Sumiyoshi³

et al. 2004

To elucidate the mechanisms underlining ␣3(V) collagen chain expression, we performed an initial analysis of the structure and function of the core promoter of the human COL5A3 gene. The core promoter, which lacks a typical TATA motif and has a high GC content, was defined within the ؊129 bp immediately upstream from the major transcription start site by transient transfection experiments. In this region, we identified four DNAprotein complexes, named A, B, C, and D, by a combination of DNase I footprinting and electrophoretic mobility shift assays. Electrophoretic mobility shift assays using mutant oligonucleotide revealed that the complexes A, B, C, and D bind to ؊122 to ؊117, the ؊101 to ؊96, the ؊83 to ؊78, and the ؊68 to ؊57 bp, respectively. The competition assays using consensus oligonucleotides and supershift assays with specific antibodies Vertebrate collagens, a large family of extracellular proteins, are critically important for the formation and function of virtually every organ system (1). Among them, fibrillar collagen, which includes five different molecular types I, II, III, V, and XI, participates in the formation of fibrils with molecules packed in quarter-staggered arrays (2, 3). The fibrillar collagens are divided into major types (I-III) and minor types (V and XI) based on their relative expression levels. Minor fibrillar collagen types V and XI are incorporated into the fibrils of the much more abundant collagen types I and II, respectively, and act as regulators of the sizes and shapes of the resultant heterotypic fibrils (4 -7). The collagen molecules are either homotrimers with ␣ chains or heterotrimers with two or three different ␣ chains. The predominant molecular form of type V is the heterotrimer [␣1(V)] 2 ␣2(V) and is expressed in most tissues (8). Other forms of type V collagen include the [␣1(V)] 3 homotrimer that is synthesized in cultures of hamster lung cells (9) and the ␣1(V)␣2(V)␣3(V) heterotrimer that can be extracted from the placenta (10 -12). Cross-type heterotrimer composed of ␣2(V) and ␣1(XI) chains is present in the rhabdomyosarcoma cell line A204 and bovine vitreous (13,14). These findings suggest that type V and type XI chains constitute a single collagen type in which different combinations of chains associate in a tissue-specific manner. Recently, a fourth chain, ␣4(V), expressed in rat Schwann cells was reported (15). This ␣ chain, which can form molecules with ␣1(V) and ␣2(V) chains, seems to be the counterpart of the mouse and human ␣3(V) chain (16).Type V collagen, which is widely expressed spatially and temporally, is expressed in the mouse embryo as early as 11 days post-coitum (17). Altered production of type V collagen is associated with some connective tissue pathology, such as inflammation, some forms of cancer, and atherosclerosis (18 -20). Characterization of the cis-acting elements and trans-acting nuclear factors that modulate correct patterns of gene expression is necessary for understanding physiological and pathological conditions. Among the collag...