Endogenous proteinases in vertebrate skeletal muscle

Drabikowski, W.; Gorecka, Alicja; Jakubiec-Puka, Anna

doi:10.1016/0020-711x(77)90128-8

Cited by 52 publications

(17 citation statements)

References 30 publications

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“…A similar proteolysis by a PMSF-inhibitable mast cell alkaline protease has also been observed during the preparation of rat cardiac myosin (Uchida et al, 1977). The tissues of rats contain especially high levels of the mast cell protease as compared to those of other mammals such as rabbits (Drabikowski et al, 1977). This dif- ference between rats and rabbits in tissue mast cell protease content correlates well with our finding that gap junctions prepared in the absence of PMSF from rabbit hearts contain polypeptides larger than Mr 28,500 (Manjunath et al, 1982a), whereas rat heart junctions isolated without PMSF are completely degraded to the Mr 29,500 polypeptide.…”

Section: Proteolysis Of Cardiac Gap Junctions During Membrane Isolationsupporting

confidence: 79%

“…This activity, most of which is presumably localized within the granules of the mast cell (Woodbury et al, 1978a,b), is described in the literature as solubilizable only in solutions of high ionic strength, e.g., 0.5 to 0.8 M phosphate (Sanada et al, 1978;Everitt & Neurath, 1979), 1.1 M K1 (Noguchi & Kandatsu, 1976) and I M KCI (Drabikowski et al, 1977;Griffin & Wildenthal, 1978). The initial homogenization step of our procedure for isolating cardiac gap junctions, during which the tissue is homogenized at low ionic strength in l mM NaHCO3, pH 8.2, would therefore fail to solubilize the protease of mast cell granules.…”

Section: Proteolysis Of Cardiac Gap Junctions During Membrane Isolationmentioning

confidence: 94%

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Proteolysis of cardiac gap junctions during their isolation from rat hearts

1985

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Gap junctions (GJ) isolated from rat hearts in presence of the protease inhibitor phenylmethylsulfonylfluoride (PMSF) contain a Mr 44,000 to 47,000 major polypeptide and have a urea-resistant layer of fuzz on their cytoplasmic surfaces, whereas junctions isolated without PMSF are proteolyzed to a Mr 29,500 polypeptide by a serine protease and have smooth cytoplasmic surfaces (C.K. Manjunath, G.E. Goings & E. Page Am. J. Physiol. 246:H865-H875, 1984). Rat liver GJ isolated with or without PMSF contain a Mr 28,000 polypeptide and have smooth cytoplasmic surfaces. Here we examine the origin, type and inhibitor sensitivity of the heart protease; why similar proteolysis is absent during isolation of rat liver gap junctions; and whether the Mr 44,000 to 47,000 cardiac GJ polypeptide is the precursor of the Mr 29,500 subunit. We show that the Mr 44,000 to 47,000 polypeptide corresponds to the unproteolyzed connexon subunit; that proteolysis of this polypeptide occurs predominantly during exposure to high ionic strength solution (0.6 M KI) which releases serine protease from mast cell granules; that this protease is inhibitable with PMSF and (less completely) soybean trypsin inhibitor and chymostatin; and that in vivo degranulation of mast cells by injecting rats with compound 48/80 fails to prevent breakdown of cardiac GJ during isolation. The results support the concept that GJ from rat heart and liver differ in protein composition.

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Section: Proteolysis Of Cardiac Gap Junctions During Membrane Isolationsupporting

confidence: 79%

Section: Proteolysis Of Cardiac Gap Junctions During Membrane Isolationmentioning

confidence: 94%

Proteolysis of cardiac gap junctions during their isolation from rat hearts

1985

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“…Alkaline proteolytic activity present in rat muscle which derives from the mast cells (2,20) was found to increase in dystrophic or denervated muscle (5,21). In the present work, however, the lack of increase of autolytic activ ity at alkaline pH after denervation or during regeneration was observed.…”

Section: Resultscontrasting

confidence: 52%

“…Figure 4 shows the dependence of autolytic activity on pH in the soleus and tibialis anterior muscles. In both muscles two maxima are pre sent, one at pH 3.0-4.0, corresponding to acid lysosomal proteases cathepsins B (EC 3.4.22.1), C (EC 3.4.14.1), D (EC 3.4.23.5) (10,11), and the second at pH 9.0-10.5, corresponding to alkaline protease (2,20). At the neutral pH region the extent of autolysis was much smal ler.…”

Section: Resultsmentioning

confidence: 99%

Influence of Denervation and Reinnervation on Autolytic Activity and on Protein Composition of Skeletal Muscle in Rat

Jakubiec-Puka¹,

Drabikowski²

1978

Enzyme

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Changes in the proteolytic activity and in the relative content of protein in soluble, myofibrillar and insoluble fractions were investigated following denervation and reinnervation of the soleus and tibialis anterior muscles of the rat. After denervation an increase of autolysis in the acid and neutral pH range, but not in the alkaline one, was found in both muscles. An increased autolysis at the acid and neutral pH range was also observed in both muscles after reinnervation, when the weight of the muscles increased. The results indicate the lack of inverse relationship between the changes of proteolytic activity and the decrease or increase of the amount of muscle proteins in the course of muscle atrophy and regeneration.

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“…Drabikowsky et al [9] proved that the course of endogenous proteolysis was to a great extent function of pH. Drabikowsky et al [9] proved that the course of endogenous proteolysis was to a great extent function of pH.…”

Section: Discussionmentioning

confidence: 99%

Investigation of the Short-Time Autolysis of Rat Hearts by Means of SDS

Vándor¹,

Varga

1979

Z Rechtsmed

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The short-time autolysis of hearts was regarded as a model of ischaemic heart failure. Therefore, isolated rat hearts were subjected to 30--120 min autolysis in a Locke solution at 37 degrees C. Electron microscopic examinations and myofibrillar preparations were made from the autolysed heart ventricles. The myofibrillar proteins were resolved by SDS-polyacrylamide gel electrophoresis. After 30 min autolysis the amount of a protein of 192,000 daltons greatly increased. At the same time on the electron micrographs the focal destruction of filament destruction on the A filament area and the mitochondrial structure altered too. After 60 min autolysis another protein of 36,400 daltons appeared. On the electron micrographs the focal desintegration of Z membranes and the focal destruction of I filaments can be observed. After 120 min autolysis further proteolytic products could not be detected by gel electrophoresis but on the electron micrographs the destruction of Z membranes and I filaments became more pronounced.

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Endogenous proteinases in vertebrate skeletal muscle

Cited by 52 publications

References 30 publications

Proteolysis of cardiac gap junctions during their isolation from rat hearts

Proteolysis of cardiac gap junctions during their isolation from rat hearts

Influence of Denervation and Reinnervation on Autolytic Activity and on Protein Composition of Skeletal Muscle in Rat

Investigation of the Short-Time Autolysis of Rat Hearts by Means of SDS

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