Cockroach Collagen: Isolation, Biochemical and Biophysical Characterization

Abstract

Collagen fibrils from the mesenteric connective sheath of the adult cockroach Periplaneta americana were extracted by enzymatic digestion with pepsin and were purified. Chromatographic studies and sodium dodecylsulfate electrophoresis revealed the presence of a single chain. It was demonstrated that the structure of this collagen could be represented by the formula (a)3. The amino acid composition is typical of collagens (one-third glycine, and a high imino acid content) and similar to that of type 11. The carbohydrate content was high (8.8%), and the cyanogen bromide pattern was different from that of known collagens. The chains were linked by the stable intermolecular bond dihydroxylysinonorleucine. The banding patterns of the segment-long-spacing crystallites and of the reconstituted fibrils were similar to type I collagen. The molecular weight ( M , 280000) and length (285 nm) were typical, but the denaturation temperature was high (38.5 "C). It was concluded that cockroach mesenteric collagen showed the characteristic features of invertebrate mesodermal collagens, except that of the thermal stability of the triple-helical structure.

Synthesis of prolyl 4-hydroxylase α subunit and type IV collagen in hemocytic granular cells of silkworm, Bombyx mori: Involvement of type IV collagen in self-defense reaction and metamorphosis

“…Previous biochemical works showed the existence of vertebrate-type type I or type II collagen-like protein in insects such as grasshopper, Locusta migratoria (Ashhurst and Bailey, 1980), and cockroach, Periplaneta americana (Francois et al, 1980). Lunstrum et al (1988) identified D. melanogaster type IV collagen (ColIV) a1(IV) chain as a basement membrane component and demonstrated that the collagen chain was synthesized in hemocytes and fat bodies.…”

Bacillus thuringiensis CbpA is a collagen binding cell surface protein under c-di-GMP control

“…The collagen content in the human intestine was found to be predominately collagen I (68%), collagen III (20%) and collagen V (12%) ( Graham et al, 1988 ), and collagen is located in the submucosa of the gastrointestinal wall, but also in the basement membrane which is attached to the overlaying epithelium and contains collagen IV ( Visser et al, 1993 , Beaulieu et al, 1994 ). Collagen is also found in invertebrates including insects, where it is located under the epidermis and around organs including the midgut, and there is evidence which supports that insect collagens are similar to mammalian collagen I and IV ( Francois et al, 1980 , Francois, 1985 , Lunstrum et al, 1988 ). The phylogenetic distribution of CbpA with its predominance in phylogenetic group IV may imply that this protein could be more abundant in B. cereus group strains isolated from non-clinical sources.…”

The multi-layered protective cuticle of Collembola: a chemical analysis

“…Furthermore, the sample showed a high amount of tyrosine and serine residues. For comparison, the amino acid compositions of structural proteins, such as fibroin (Bombyx mori), collagen (Periplaneta americana) and resilin (Schistocerca gregaria) [30][31][32] are included in table 2. A common feature of structural proteins, glycine was the dominating amino acid in all proteins.…”