Increased Histaminase Activity in
the Atrophie Muscle of Denervated Frog

Rv, Krishnamoorthy

doi:10.1159/000458773

Cited by 3 publications

(2 citation statements)

References 9 publications

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“…The assay mixture corttaining 1 ml of dialysate, 1 ml of 1~ casein (w/v) irt 0.0005 M sodium bicarbonate artd 1 ml of 0-1 M CaCI2 was incubated at 37 ° C for 3 hr. The assay method was adapted from Krishnamoorthy (1971). The reactiort at the end of incubation period was stopped by adding 2 ml of ice cold 10~ TCA, the resultartt mixture was centrifuged ao.d the amio.o acid content of the supcmatant was determio.ed as usual (Moore and Stein 1954).…”

Section: Proteolytic Activitymentioning

confidence: 99%

“…These different activities are achieved by the trophic influences of the innervating nerves. The fact that lysosomes change/increase during neuro-muscutar pathological conditions like hereditary muscular dystrophy (Tappel et al 1962), denervation atrophy (Pollack and Bird 1968;Krishnamoorthy 1971Krishnamoorthy , 1972 and also during vitamin E deficiency (Bond and Bird 1966) demonstrate that they are u~der the control of trophic influertces of the nerve. Many muscle enzymes like actomyosin ATPase respond to functional demands in muscles (Gutmann et al 1971 ;Guth and Wells 1972).…”

Section: Muscles Exhibiting Compensatory Proteolytic Activio'mentioning

confidence: 99%

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Some aspects of protein metabolism in the skeletal muscles of frog (Rana cyanophlictis) during cold acclimation

Sridhara

1979

Proc. Indian Acad. Sci.

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Abstract. In spite of great.evidence of increased protein synthesis during cold acclimation in many poikilotherms, little is known about protein turnover rates during thermal stress. Studies on protein levels and its catabolism in the different skeletal muscles of Rana cyanopMictis revealed muscle specific compensation to temperature.The variability in the adaptation of different muscles is attributed to trophic influences of the nervous system primarily and secondarily to acclimation.

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Section: Proteolytic Activitymentioning

confidence: 99%

Section: Muscles Exhibiting Compensatory Proteolytic Activio'mentioning

confidence: 99%

Some aspects of protein metabolism in the skeletal muscles of frog (Rana cyanophlictis) during cold acclimation

Sridhara

1979

Proc. Indian Acad. Sci.

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References

1983

Amine Oxidases in Clinical Research

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A Class III PDZ Binding Motif in the Myotilin and FATZ Families Binds Enigma Family Proteins: a Common Link for Z-Disc Myopathies

Nandelstadh

Ismail

Gardin

et al. 2009

Molecular and Cellular Biology

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Interactions between Z-disc proteins regulate muscle functions and disruption of these interactions results in muscle disorders. Mutations in Z-disc components myotilin, ZASP/Cypher, and FATZ-2 (calsarcin-1/ myozenin-2) are associated with myopathies. We report here that the myotilin and the FATZ (calsarcin/ myozenin) families share high homology at their final C-terminal five amino acids. ThisL motif is present almost exclusively in these families and is evolutionary conserved. We show by in vitro and in vivo studies that proteins from the myotilin and FATZ (calsarcin/myozenin) families interact via this novel type of class III PDZ binding motif with the PDZ domains of ZASP/Cypher and other Enigma family members: ALP, CLP-36, and RIL. We show that the interactions can be modulated by phosphorylation. Calmodulin-dependent kinase II phosphorylates the C terminus of FATZ-3 (calsarcin-3/myozenin-3) and myotilin, whereas PKA phosphorylates that of FATZ-1 (calsarcin-2/myozenin-1) and FATZ-2 (calsarcin-1/ myozenin-1). This is the first report of a binding motif common to both the myotilin and the FATZ (calsarcin/ myozenin) families that is specific for interactions with Enigma family members.The sarcomere of striated muscle consists of strictly organized subunits, myosin-containing thick filaments and actincontaining thin filaments. The thin filaments are aligned and cross-linked at the Z-discs by a molecular complex in which ␣-actinin is one of the core structures. Since the contractile force is transduced via the Z-discs, this structure has special requirements. It must provide extensive stability and yet undergo modulation in response to external signals. The Z-discs also serve as important sensors of extracellular cues and mediators of cellular signals that result in various adaptive responses (37). Muscle cells are able to sense changes in their workload and adapt accordingly via complex signaling pathways, some involving calcium, since its level in muscle cells alters in response to nerve pulses and muscle contraction. Of special importance is calcineurin, a sarcomeric calcium/calmodulin-dependent phosphatase that can act as a sensor of change. It is involved in the regulation of genes affecting muscle differentiation and fiber-type specification (12, 13).The special role of the Z-discs is indicated by the fact that mutations in several Z-disc proteins can result in neuromuscular disorders and cardiomyopathies. For instance, myofibrillar myopathy (desmin-related myopathy), a disease characterized by sarcomere disintegration and accumulation of thin filament material, is caused by dominantly inherited missense mutations in Z-disc proteins: myotilin, filamin-C, and Z-band alternatively spliced PDZ motif-containing protein (ZASP, also named LIM domain-binding factor 3, Cypher, or Oracle) (42, 43, 52). Missense mutations in myotilin can also result in limbgirdle muscular dystrophy 1A and spheroid body myositis (10, 18), while mutations in ZASP/Cypher (8, 57), myopalladin or FATZ-2 (calsarcin-1/myozenin-2) have been ...

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Increased Histaminase Activity in the Atrophie Muscle of Denervated Frog

Cited by 3 publications

References 9 publications

Some aspects of protein metabolism in the skeletal muscles of frog (Rana cyanophlictis) during cold acclimation

Some aspects of protein metabolism in the skeletal muscles of frog (Rana cyanophlictis) during cold acclimation

References

A Class III PDZ Binding Motif in the Myotilin and FATZ Families Binds Enigma Family Proteins: a Common Link for Z-Disc Myopathies

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