PMID- 9180271
OWN - NLM
STAT- MEDLINE
DCOM- 19970627
LR  - 20190621
IS  - 0014-5793 (Print)
IS  - 0014-5793 (Linking)
VI  - 408
IP  - 1
DP  - 1997 May 12
TI  - Different actin affinities of human cardiac essential myosin light chain 
      isoforms.
PG  - 71-4
AB  - The N terminus of myosin light chain 1 (MLC-1) of skeletal muscle bind to the C 
      terminus of actin. We investigated whether the N termini of human cardiac MLC-1 
      isoforms likewise bind to actin. Furthermore, we investigated whether the 
      N-terminal sequence 5-15 (P5-14) of MLC-1 of human atrium (ALC-1) and ventricle 
      (VLC-1) bind with different affinities to actin. Affinity beads were produced by 
      covalently coupling a synthetic peptide corresponding to the N-terminal sequence 
      4-14 of human VLC-1 to aminohexylagarose in order to bind G-actin. We found, that 
      G-actin specifically binds to the affinity beads. Furthermore, preincubation of 
      G-actin with P5-14 of both ALC-1 and VLC-1 decreased the amount of G-actin 
      recovered from the affinity beads in a concentration-dependent manner. The 
      half-maximal effective concentrations, however were significantly (p < 0.01) 
      different being 0.32 +/- 0.02 microM and 0.71 +/- 0.02 microM for the VLC-1 and 
      ALC-1 peptide, respectively. The appropriate scrambled peptides were without 
      effect up to 3 microM. These results demonstrate the specific interaction between 
      the N-terminal domains of human cardiac MLC-1 isoforms and actin and reveal 
      different actin affinities of MLC-1 isoforms. Weak binding of ALC-1 to actin 
      could explain the higher cycling kinetics of cross-bridges with ALC-1 compared to 
      those with VLC-1.
FAU - Morano, I
AU  - Morano I
AD  - Max-Delbruck Center for Molecular Medicine, Berlin-Buch, Germany.
FAU - Haase, H
AU  - Haase H
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - FEBS Lett
JT  - FEBS letters
JID - 0155157
RN  - 0 (Actins)
RN  - 0 (Myosin Light Chains)
RN  - 0 (Peptide Fragments)
RN  - 0 (myosin light chain I)
RN  - 58856-73-8 (aminohexyl-sepharose)
RN  - 9012-36-6 (Sepharose)
SB  - IM
MH  - Actins/*metabolism
MH  - Blotting, Western
MH  - Chromatography, Affinity
MH  - Heart Atria/chemistry
MH  - Heart Ventricles/chemistry
MH  - Humans
MH  - Myocardium/*chemistry
MH  - Myosin Light Chains/chemistry/*metabolism
MH  - Peptide Fragments/chemistry/metabolism
MH  - Protein Binding
MH  - Sepharose/analogs & derivatives/metabolism
EDAT- 1997/05/12 00:00
MHDA- 1997/05/12 00:01
CRDT- 1997/05/12 00:00
PHST- 1997/05/12 00:00 [pubmed]
PHST- 1997/05/12 00:01 [medline]
PHST- 1997/05/12 00:00 [entrez]
AID - S0014-5793(97)00390-6 [pii]
AID - 10.1016/s0014-5793(97)00390-6 [doi]
PST - ppublish
SO  - FEBS Lett. 1997 May 12;408(1):71-4. doi: 10.1016/s0014-5793(97)00390-6.