Shohshi Mizuta

Two genetically distinct types of collagen in kuruma prawn penaeus japonicus

Abstract 1. 1. At least three types of collagen was found in the muscle of kuruma prawn Penaeus japonicus . Two of them, called AR-I and AR-II collagens, were isolated from the pepsin-solubilized collagen. 2. 2. The subunit composition of AR-I collagen, major molecular species, was proved to be (α I) 3 homotrimer. Its amino acid composition was similar to that of Type V collagen rather than Type I collagen. 3. 3. AR-II collagen, minor molecular species, was found to have disulfide bonds in the molecule. Its amino acid composition was similar to that of AR-I collagen. The sodium dodecyl sulfate-polyacrylamide gel electrophoresis pattern of AR-II collagen suggested the complexes of its structure.

Isolation and partial characterization of a new alpha component of collagen from muscle of kuruma prawn Penaeus japonicus

Abstract 1. 1. A new α component, α2(Pr), was successfully isolated from the pepsin-solubilized collagen from the muscle of kuruma prawn. 2. 2. The component α2(Pr) was genetically distinct from components comprising Type AR-I and AR-II collagens by peptide mapping with proteases, amino acid analysis, and immunoblotting, and had high contents of leucine and hydroxylsine, and a low content of alanine. 3. 3. The effect of pepsin digestion on the molecule containing the α2(Pr) component was examined by using immunological techniques. The component α2(Pr) in intact form consisted of several types of components. Although they were all identical to each other in the helical region, each of them had a distinct form of non-helical region with a slight modification.

Immunohistochemical localization of genetically distinct types of collagen in muscle of kuruma prawn Penaeus japonicus

Abstract 1. 1. The location of genetically distinct types of collagen in muscular tissue of the kuruma prawn was examined using immunohistochemical techniques. 2. 2. Collagen was distributed not only in muscle connective tissues, which were classified into three forms, epimysium, perimysium and endomysium, but also in subcuticular membrane, which was mainly composed of two layers, hypodermis and subcuticular connective tissue. 3. 3. The α1(Pr) component existed in all connective tissues in the kuruma prawn muscle. Type AR-II collagen was distributed in all the connective tissues except for the hypodermis, while the α2(Pr) component existed in the thin connective tissues, the perimysium and endomysium, and in the hypodermis.

THE IMMUNOLOGICAL STUDY ON THE EFFECT OF PEPSIN DIGESTION ON GENETICALLY DISTINCT TYPES OF COLLAGEN IN MUSCLE OF KURUMA PRAWN PENAEUS JAPONICUS

Abstract 1. 1. The effect of pepsin digestion on each type of collagen from the muscle of kuruma prawn Penaeus japonicus was examined by immunological techniques. 2. 2. The major collagen (named type AR-I) in intact form comprised of several types of α-components. Although they were all identical to each other in the helical region, each of them had a distinct form of non-helical domain with a slight modification. 3. 3. The minor collagen (named type AR-II) in intact form had the large non-helical domain sensitive to pepsin digestion and disulfide bonds in its molecule. 4. 4. Another type of minor collagen was proved to be present in the prawn muscle.

Characterization of collagen in muscle of several crustacean species

Abstract Properties of the collagens in the muscles of 16 species of crustaceans were examined in association with their movements or behavioral modes. It was suggested that Type AR-I and AR-II collagens were distributed widely among crustacean species. The results of peptide mapping and immunoblotting analyses suggested a considerable difference in the primary structure of collagen among species. Total collagen content varied among species, ranging from 0.04 to 0.58% of wet tissue and from 0.4 to 3.5% of total tissue protein. In addition, there seemed to be a considerable difference in the relative proportion of the α2(Cr) (Cr: crustacean) component to the total collagen among species.

Subunit composition of distinct types of collagens in the muscle of the kuruma prawn Penaeus japonicus

Abstract 1. 1. The subunit composition of the collagen molecules containing two α components, α1(Pr) and α2(Pr), in kuruma prawn muscle were examined. 2. 2. Three molecular forms of collagen, [α1(Pr)]3, [α1(Pr)]2α2(Pr) and α1(Pr)[α2(Pr)]2, were proved to be present. They were named Type AI-Ia, AR-Ib and AR-Ic, respectively. 3. 3. Type AR-II collagen was suggested to be a heterotrimer having a pepsin-sensitive region in the helical domain.

CHARACTERIZATION OF A MAJOR ALPHA COMPONENT OF COLLAGEN FROM MUSCLE OF ANTARCTIC KRILL EUPHAUSA SUPERBA

Abstract A major α component of collagen was isolated from the muscle of the Antarctic krill Euphausia superba by SP-Toyopearl column chromatography. Its characteristics were examined by biochemical and immunohistochemical techniques. The major α component of the krill collagen, referred to as α 1(Kr) component, occupied more than 80% of the total pepsin-solubilized collagen and showed typical compositional feature of crustacean major collagens, with low and high contents of alanine and hydroxylysine, respectively. The α 1(Kr) component was mainly distributed in relatively thick connective tissues, epimysium and perimysium. These results suggest that the α 1(Kr) component may functionally correspond to the major α component of collagen in decapods, α 1(AR-I) (AR-I: Arthropod-Type I), and comprise a major homotrimeric collagen molecule, [ α 1(AR-I) 3 ].