Abstract
We describe the changes in proportions of myofibrillar proteins elicited by chronic congestive heart failure in the costal diaphragm (DIA) of humans using one and two-dimensional electrophoretic techniques. Three myosin heavy chain (MHC) isoforms were found in the DIA from control subjects: slow MHC I (43 ± S.E. 2%), fast MHC IIa (41 ± 2%) and fast MHC IIb (17 ± 1%). In heart failure DIA, the percentage of MHC I was increased to 57 ± 2%, while that of MHC IIb was decreased to 8 ± 2 (P < 0.001 for both cases). Similarly, this DIA had higher molar ratios (%) of the slow myosin light chain isoforms (i.e. 1sa, 1sb, and 2s), and lower molar ratios of the fast isoforms (i.e. If, 2f, and 3f) than control DIA. Heart failure DIA also contained lower proportions of both α-tropomyosin and fast isoforms of troponin-T, I and C than control DIA. These results indicate that heart failure elicits fast-to-slow transformations of both myosin and regulatory proteins of human costal DIA. These changes can be viewed as an increase in slow-twitch characteristics of the DIA and differ from the adaptations elicited by heart failure in limb muscles.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 2537-2541 |
| Number of pages | 5 |
| Journal | Journal of Molecular and Cellular Cardiology |
| Volume | 28 |
| Issue number | 12 |
| DOIs | |
| State | Published - Dec 1996 |
| Externally published | Yes |
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Keywords
- Heart failure
- Human diaphragm
- Myofibrillar proteins
- Myosin heavy chain isoforms
- Troponin-tropomyosin regulatory complex
ASJC Scopus subject areas
- Molecular Biology
- Cardiology and Cardiovascular Medicine
Cite this
Changes in myofibrillar protein composition of human diaphragm elicited by congestive heart failure. / Tikunov, B. A.; Mancini, D.; Levine, Stephanie M.
In: Journal of Molecular and Cellular Cardiology, Vol. 28, No. 12, 12.1996, p. 2537-2541.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Changes in myofibrillar protein composition of human diaphragm elicited by congestive heart failure
AU - Tikunov, B. A.
AU - Mancini, D.
AU - Levine, Stephanie M
PY - 1996/12
Y1 - 1996/12
N2 - We describe the changes in proportions of myofibrillar proteins elicited by chronic congestive heart failure in the costal diaphragm (DIA) of humans using one and two-dimensional electrophoretic techniques. Three myosin heavy chain (MHC) isoforms were found in the DIA from control subjects: slow MHC I (43 ± S.E. 2%), fast MHC IIa (41 ± 2%) and fast MHC IIb (17 ± 1%). In heart failure DIA, the percentage of MHC I was increased to 57 ± 2%, while that of MHC IIb was decreased to 8 ± 2 (P < 0.001 for both cases). Similarly, this DIA had higher molar ratios (%) of the slow myosin light chain isoforms (i.e. 1sa, 1sb, and 2s), and lower molar ratios of the fast isoforms (i.e. If, 2f, and 3f) than control DIA. Heart failure DIA also contained lower proportions of both α-tropomyosin and fast isoforms of troponin-T, I and C than control DIA. These results indicate that heart failure elicits fast-to-slow transformations of both myosin and regulatory proteins of human costal DIA. These changes can be viewed as an increase in slow-twitch characteristics of the DIA and differ from the adaptations elicited by heart failure in limb muscles.
AB - We describe the changes in proportions of myofibrillar proteins elicited by chronic congestive heart failure in the costal diaphragm (DIA) of humans using one and two-dimensional electrophoretic techniques. Three myosin heavy chain (MHC) isoforms were found in the DIA from control subjects: slow MHC I (43 ± S.E. 2%), fast MHC IIa (41 ± 2%) and fast MHC IIb (17 ± 1%). In heart failure DIA, the percentage of MHC I was increased to 57 ± 2%, while that of MHC IIb was decreased to 8 ± 2 (P < 0.001 for both cases). Similarly, this DIA had higher molar ratios (%) of the slow myosin light chain isoforms (i.e. 1sa, 1sb, and 2s), and lower molar ratios of the fast isoforms (i.e. If, 2f, and 3f) than control DIA. Heart failure DIA also contained lower proportions of both α-tropomyosin and fast isoforms of troponin-T, I and C than control DIA. These results indicate that heart failure elicits fast-to-slow transformations of both myosin and regulatory proteins of human costal DIA. These changes can be viewed as an increase in slow-twitch characteristics of the DIA and differ from the adaptations elicited by heart failure in limb muscles.
KW - Heart failure
KW - Human diaphragm
KW - Myofibrillar proteins
KW - Myosin heavy chain isoforms
KW - Troponin-tropomyosin regulatory complex
UR - http://www.scopus.com/inward/record.url?scp=17144470129&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=17144470129&partnerID=8YFLogxK
U2 - 10.1006/jmcc.1996.0245
DO - 10.1006/jmcc.1996.0245
M3 - Article
C2 - 9004169
AN - SCOPUS:17144470129
VL - 28
SP - 2537
EP - 2541
JO - Journal of Molecular and Cellular Cardiology
JF - Journal of Molecular and Cellular Cardiology
SN - 0022-2828
IS - 12
ER -