The avian low score normal muscle weakness alters decorin expression and collagen crosslinking

被引:43
作者
Velleman, SG
Yeager, JD
Krider, H
Carrino, DA
Zimmerman, SD
McCormick, RJ
机构
[1] UNIV CONNECTICUT,DEPT ANIM GENET,STORRS,CT 06269
[2] UNIV CONNECTICUT,DEPT MOLEC & CELL BIOL,STORRS,CT 06269
[3] UNIV WYOMING,DEPT ANIM SCI,LARAMIE,WY 82071
[4] CASE WESTERN RESERVE UNIV,DEPT BIOL,CLEVELAND,OH 44106
关键词
decorin; proteoglycan; collagen; skeletal muscle; myogenesis;
D O I
10.3109/03008209609028891
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Extracellular matrix development of chicken pectoral muscle was examined in the Low Score Normal (LSN) genetic muscle weakness and compared to both normal and avian muscular dystrophy (MD). At 20 days of embryonic development significant elevations were noted in LSN total glycosaminoglycan concentration and decorin, while at 14 days, LSN glycosaminoglycan and decorin levels were indistinguishable from the controls. Levels of a large skeletal muscle chondroitin sulfate proteoglycan (M-CSPG) appeared to be unaffected. Morphologically, at 20 days, the extracellular matrix space between muscle fibers increased to a level characteristic to that observed in avian muscular dystrophy. At six weeks posthatch a marked increase in LSN collagen crosslinking relative to MD or control tissues was observed while collagen concentration was not altered. By one year posthatch LSN collagen crosslink levels did not significantly differ from normal tissue. These data support the concept that the LSN muscle weakness is associated with changes in both proteoglycan and collagen characteristics.
引用
收藏
页码:33 / 39
页数:7
相关论文
共 35 条
[1]   MEAT TENDERNESS - IMMUNOFLUORESCENT LOCALIZATION OF THE ISOMORPHIC FORMS OF COLLAGEN IN BOVINE MUSCLES OF VARYING TEXTURE [J].
BAILEY, AJ ;
RESTALL, DJ ;
SIMS, TJ ;
DUANCE, VC .
JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, 1979, 30 (02) :203-210
[2]  
BASSOLS A, 1988, J BIOL CHEM, V263, P3039
[3]  
BINETTE F, 1994, J BIOL CHEM, V269, P19116
[4]  
BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3
[5]   MOLECULAR-BIOLOGY OF MUSCLE DEVELOPMENT [J].
BUCKINGHAM, M .
CELL, 1994, 78 (01) :15-21
[6]   STRUCTURAL CHARACTERIZATION OF CHICK EMBRYONIC SKELETAL-MUSCLE CHONDROITIN SULFATE PROTEOGLYCAN [J].
CARRINO, DA ;
CAPLAN, AI .
CONNECTIVE TISSUE RESEARCH, 1989, 19 (01) :35-50
[7]   IDENTITY OF THE CORE PROTEINS OF THE LARGE CHONDROITIN SULFATE PROTEOGLYCANS SYNTHESIZED BY SKELETAL-MUSCLE AND PRECHONDROGENIC MESENCHYME [J].
CARRINO, DA ;
DENNIS, JE ;
DRUSHEL, RF ;
HAYNESWORTH, SE ;
CAPLAN, AI .
BIOCHEMICAL JOURNAL, 1994, 298 :51-60
[8]  
COSMOS E, 1979, FACTORS INFLUENCE PH, P571
[9]   DECORIN AND A LARGE DERMATAN SULFATE PROTEOGLYCAN IN BOVINE STRIATED-MUSCLE [J].
EGGEN, KH ;
MALMSTROM, A ;
KOLSET, SO .
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY, 1994, 1204 (02) :287-297
[10]   QUANTITATION OF HYDROXYPYRIDINIUM CROSSLINKS IN COLLAGEN BY HIGH-PERFORMANCE LIQUID-CHROMATOGRAPHY [J].
EYRE, DR ;
KOOB, TJ ;
VANNESS, KP .
ANALYTICAL BIOCHEMISTRY, 1984, 137 (02) :380-388