The evolution of fibrillar collagens: a sea-pen collagen shares common features with vertebrate type V collagen.
The extracellular matrix of marine primitive invertebrates (sponges, polyps and jellyfishes) contains collagen fibrils with narrow diameters. From various data, it has been hypothesized that these primitive collagens could represent ancestral forms of the vertebrate minor collagens, i.e., types V or XI. Recently we have isolated a primitive collagen from the soft tissues of the sea-pen Veretillum cynomorium. This report examines whether the sea-pen collagen shares some features with vertebrate type V collagen. Rotary shadowed images of acid-soluble collagen molecules extracted from beta-APN treated animals, positive staining of segment-long-spacing crystallites precipitated from pepsinized collagen, Western blots of the pepsinized alpha1 and alpha2 chains with antibodies to vertebrate types I, III and V collagens, and in situ gold immunolabeling of ECM collagen fibrils were examined. Our results showed that the tissue form of the sea-pen collagen is a 340-nm threadlike molecule, which is close to the vertebrate type V collagen with its voluminous terminal globular domain, the distribution of most of its polar amino-acid residues, and its antigenic properties.
Tillet
E
E
Institut de Biologie et Chimie des Protéines, Lyon, France.
Franc
J M
JM
Franc
S
S
Garrone
R
R
D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies; D003094:Collagen / Q000737:chemistry* / Q000302:isolation & purification / Q000648:ultrastructure; D049832:Decapodiformes / Q000737:chemistry*; D005260:Female; D006801:Humans; D008854:Microscopy, Electron; D016253:Microscopy, Immunoelectron; D008969:Molecular Sequence Data; D010434:Pepsin A; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification; D010920:Placenta / Q000737:chemistry; D011247:Pregnancy; D051381:Rats; D014714:Vertebrates
D000906:Antibodies; D010446:Peptide Fragments; D003094:Collagen; D010434:Pepsin A