Biomaterial Database

Calcium-binding protein, parvalbumin, is reduced in mutant mammalian muscle with abnormal contractile properties. 1984

I Stuhlfauth, and J Reininghaus, and H Jockusch, and C W Heizmann

To elucidate the biochemical basis of hereditary muscle diseases in an experimental mammal, we performed polypeptide analyses on skeletal muscles of neuromuscular mutants of the mouse. In one of these, "arrested development of righting response" (adr), the concentration of the soluble Ca2+-binding protein parvalbumin was drastically reduced in comparison to wild type. This reduction was not an unspecific consequence of muscle disease, as it was not observed in two other neuromuscular mouse mutants, "wobbler" (wr) and "motor endplate disease" (med or medjo). Isometric twitches of adr muscle had only slightly prolonged contraction and half-relaxation times, yet long-lasting after-contractions were observed upon repeated (20-100 Hz) direct stimulation. Thus, parvalbumin may be mainly involved in the relaxation after tetanic contraction of fast-twitch fibers.

UI	MeSH Term	Description	Entries
D007526	Isoelectric Point	The pH in solutions of proteins and related compounds at which the dipolar ions are at a maximum.	Isoelectric Points,Point, Isoelectric,Points, Isoelectric
D008817	Mice, Mutant Strains	Mice bearing mutant genes which are phenotypically expressed in the animals.	Mouse, Mutant Strain,Mutant Mouse Strain,Mutant Strain of Mouse,Mutant Strains of Mice,Mice Mutant Strain,Mice Mutant Strains,Mouse Mutant Strain,Mouse Mutant Strains,Mouse Strain, Mutant,Mouse Strains, Mutant,Mutant Mouse Strains,Mutant Strain Mouse,Mutant Strains Mice,Strain Mouse, Mutant,Strain, Mutant Mouse,Strains Mice, Mutant,Strains, Mutant Mouse
D008970	Molecular Weight	The sum of the weight of all the atoms in a molecule.	Molecular Weights,Weight, Molecular,Weights, Molecular
D009119	Muscle Contraction	A process leading to shortening and/or development of tension in muscle tissue. Muscle contraction occurs by a sliding filament mechanism whereby actin filaments slide inward among the myosin filaments.	Inotropism,Muscular Contraction,Contraction, Muscle,Contraction, Muscular,Contractions, Muscle,Contractions, Muscular,Inotropisms,Muscle Contractions,Muscular Contractions
D009124	Muscle Proteins	The protein constituents of muscle, the major ones being ACTINS and MYOSINS. More than a dozen accessory proteins exist including TROPONIN; TROPOMYOSIN; and DYSTROPHIN.	Muscle Protein,Protein, Muscle,Proteins, Muscle
D009132	Muscles	Contractile tissue that produces movement in animals.	Muscle Tissue,Muscle,Muscle Tissues,Tissue, Muscle,Tissues, Muscle
D009154	Mutation	Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.	Mutations
D010320	Parvalbumins	Low molecular weight, calcium binding muscle proteins. Their physiological function is possibly related to the contractile process.	Parvalbumin,Parvalbumin B
D010446	Peptide Fragments	Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.	Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia