Abstract
We found that β-actinin isoforms are present in various types of tissues in adult chicken by using immunoblotting after two dimensional gel electrophoresis; for this purpose, an antibody was raised against β-actinin purified from adult chicken breast muscle (pectoralis major). One of the β-actinin subunits, βI, was present in all tissues we examined, i.e. skeletal (pectoralis major, semitendinosus, and anterior latissimus dorsi), cardiac, and smooth (gizzard) muscles, non-muscle (brain, liver, and kidney) tissues and blood, whereas another subunit, β11, was present only in muscle tissues. A new subunit (designated βIII) that was found in the embryonic stages of skeletal muscle (Asami, Funatsu & Ishiwata (1988) J. Biochem. 103, 72-75) was present instead of βII in non-muscle tissues and blood. In cardiac and smooth muscles, βIII coexisted with βI and βII. The antibody of β-actinin did not cross-react to cytoplasmic β-actinin (molecular weight, 80, 000 daltons) found in kidney. It was suggested that the combination of βI and βIII present in non-muscle tissues and blood is identical to the barbed end capping protein isolated from brain by Killiman and Isenberg (EMBO J. 1,889-894 (1982)). It is likely that β-actinin forms a genetic family whose constituents have an ability to cap either the pointed or barbed end of actin filaments.
| Original language | English |
|---|---|
| Pages (from-to) | 76-80 |
| Number of pages | 5 |
| Journal | Journal of Biochemistry |
| Volume | 103 |
| Issue number | 1 |
| Publication status | Published - 1988 Jan |
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ASJC Scopus subject areas
- Statistics, Probability and Uncertainty
- Applied Mathematics
- Physiology (medical)
- Radiology Nuclear Medicine and imaging
- Molecular Biology
- Biochemistry
Cite this
β-actinin isoforms in various types of muscle and non-muscle tissues. / Asami, Yoko; Funatsu, Takashi; Ishiwata, Shin'ichi.
In: Journal of Biochemistry, Vol. 103, No. 1, 01.1988, p. 76-80.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - β-actinin isoforms in various types of muscle and non-muscle tissues
AU - Asami, Yoko
AU - Funatsu, Takashi
AU - Ishiwata, Shin'ichi
PY - 1988/1
Y1 - 1988/1
N2 - We found that β-actinin isoforms are present in various types of tissues in adult chicken by using immunoblotting after two dimensional gel electrophoresis; for this purpose, an antibody was raised against β-actinin purified from adult chicken breast muscle (pectoralis major). One of the β-actinin subunits, βI, was present in all tissues we examined, i.e. skeletal (pectoralis major, semitendinosus, and anterior latissimus dorsi), cardiac, and smooth (gizzard) muscles, non-muscle (brain, liver, and kidney) tissues and blood, whereas another subunit, β11, was present only in muscle tissues. A new subunit (designated βIII) that was found in the embryonic stages of skeletal muscle (Asami, Funatsu & Ishiwata (1988) J. Biochem. 103, 72-75) was present instead of βII in non-muscle tissues and blood. In cardiac and smooth muscles, βIII coexisted with βI and βII. The antibody of β-actinin did not cross-react to cytoplasmic β-actinin (molecular weight, 80, 000 daltons) found in kidney. It was suggested that the combination of βI and βIII present in non-muscle tissues and blood is identical to the barbed end capping protein isolated from brain by Killiman and Isenberg (EMBO J. 1,889-894 (1982)). It is likely that β-actinin forms a genetic family whose constituents have an ability to cap either the pointed or barbed end of actin filaments.
AB - We found that β-actinin isoforms are present in various types of tissues in adult chicken by using immunoblotting after two dimensional gel electrophoresis; for this purpose, an antibody was raised against β-actinin purified from adult chicken breast muscle (pectoralis major). One of the β-actinin subunits, βI, was present in all tissues we examined, i.e. skeletal (pectoralis major, semitendinosus, and anterior latissimus dorsi), cardiac, and smooth (gizzard) muscles, non-muscle (brain, liver, and kidney) tissues and blood, whereas another subunit, β11, was present only in muscle tissues. A new subunit (designated βIII) that was found in the embryonic stages of skeletal muscle (Asami, Funatsu & Ishiwata (1988) J. Biochem. 103, 72-75) was present instead of βII in non-muscle tissues and blood. In cardiac and smooth muscles, βIII coexisted with βI and βII. The antibody of β-actinin did not cross-react to cytoplasmic β-actinin (molecular weight, 80, 000 daltons) found in kidney. It was suggested that the combination of βI and βIII present in non-muscle tissues and blood is identical to the barbed end capping protein isolated from brain by Killiman and Isenberg (EMBO J. 1,889-894 (1982)). It is likely that β-actinin forms a genetic family whose constituents have an ability to cap either the pointed or barbed end of actin filaments.
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M3 - Article
C2 - 3360764
AN - SCOPUS:0023877405
VL - 103
SP - 76
EP - 80
JO - Journal of Biochemistry
JF - Journal of Biochemistry
SN - 0021-924X
IS - 1
ER -