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Physiological and pathological changes in levels of the two small stress proteins, HSP27 and alpha B crystallin, in rat hindlimb muscles.

Physiological and pathological changes in levels of the two small stress proteins, HSP27 and alpha B crystallin, in rat hindlimb muscles. Research Abstract Details 

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  • Physiological and pathological changes in levels of the two small stress proteins, HSP27 and alpha B crystallin, in rat hindlimb muscles. Abstract Text:

    y inagumaY Inaguma,s gotoS Goto,h shinoharaH Shinohara,k hasegawaK Hasegawa,k ohshimaK Ohshima,k katoK Kato,

    The two small stress proteins, HSP27 and alpha B crystallin, are expressed widely in normal rat tissues and abundantly in skeletal muscle. In order to clarify the physiological significance of these stress proteins, the changes in their levels were determined immunochemically, in the slow-twitch soleus muscle and fast-twitch extensor digitorum longus muscle or rectus femoris muscle of growing rats, and in those of adult rats during denervation and tenotomy. HSP27 was quantitated by specific immunoassay, similar to that for alpha B crystallin, with antibodies raised in rabbits against purified rat HSP27. In adult rats, HSP27 was present at high levels in tissues composed of striated muscle, and it was present at much higher levels in the soleus muscle than in the rectus femoris or extensor digitorum longus muscle, as is alpha B crystallin. However, in rats of perinatal age (from prenatal day 2 to postnatal day 3), levels of HSP27 in the rectus femoris muscle were enhanced like those in the soleus muscle, reaching the maximum levels at postnatal day 3. Thereafter HSP27 in the fast-twitch muscle showed a steep decrease. The increase in alpha B crystallin in the hindlimb muscles was also observed in the perinatal period. However, alpha B crystallin concentrations in the soleus muscle of perinatal rats were as low as those in rectus femoris muscle. The transection of the sciatic nerve resulted in decreases in the levels of HSP27 and alpha B crystallin in the soleus muscle of adult rats, together with increases in the levels of the two proteins in the extensor digitorum longus muscle.(ABSTRACT TRUNCATED AT 250 WORDS)

    Physiological and pathological changes in levels of the two small stress proteins, HSP27 and alpha B crystallin, in rat hindlimb muscles. Publishing Authors By Initials

    y inagumaY Inaguma,s gotoS Goto,h shinoharaH Shinohara,k hasegawaK Hasegawa,k ohshimaK Ohshima,k katoK Kato,

    For similar investigative techniques: genetic techniques: sequence alignment research abstracts see: investigative techniques: genetic techniques: sequence alignment research

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    Physiological and pathological changes in levels of the two small stress proteins, HSP27 and alpha B crystallin, in rat hindlimb muscles. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Journal of biochemistry

    VOLUME: 114

    Page Numbers: 378-84

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Sep

    YEAR: 1993

    Physiological and pathological changes in levels of the two small stress proteins, HSP27 and alpha B crystallin, in rat hindlimb muscles. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Physiological and pathological changes in levels of the two small stress proteins, HSP27 and alpha B crystallin, in rat hindlimb muscles. Keywords Mesh Terms:

    KEYWORDS: Sequence Alignment

    MESH TERMS: metabolism

    Chemical & Substance for Abstract: Physiological and pathological changes in levels of the two small stress proteins, HSP27 and alpha B crystallin, in rat hindlimb muscles. Information

    Substance Name: Muscle Proteins

    Registry Number: 0

    Grant and Affiliation Information for Physiological and pathological changes in levels of the two small stress proteins, HSP27 and alpha B crystallin, in rat hindlimb muscles.

    AFFILIATION: Department of Biochemistry, Aichi Prefectural Colony.

    Country: JAPAN

    JAPAN Research PublicationJAPAN Research Publication

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    MEDLINETA: J Biochem

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