New insight into the functional role of myorod.

In this paper, we present a refined version of the previously proposed suspension contractile model based on catch muscle proteins of the Gray's mussel (Crenomytilus grayanus). The objective of this model was to test the current hypotheses about the catch state, a unique phenomenon observed in the adductor muscle of bivalve molluscs. This state allows the muscle to maintain the force developed by contraction for a long time with minimum energy expenditure.

Does muscle-type myosin have ADPase activity?

Adenosine diphosphate (ADP) is a nucleotide that is structurally very similar to ATP but lacks one of the two high-energy bonds due to hydrolysis. In muscle studies, ADP is usually considered exclusively as a product formed during myosin cross-bridge cycling and is not otherwise involved in this process. In our study, we question the widely held view of ADP as a final product formed during muscle contraction.

Gelsolin from mussel's catch muscle.

Proteins of the gelsolin family are Ca2+-dependent, multifunctional, actin-binding proteins containing three (S1-S3, about 40 kDa) or six (S1-S6, about 80 kDa) highly conserved repeats in the amino acid sequence. The pattern of interaction of these proteins with actin is complex: they can sever actin filaments; promote polymer nucleation after binding to two actin monomers; and cap the growing barbed end of actin filaments. In the present study, an actin polymerizing factor (46 kDa) from the adductor muscle of a bivalve mollusc has been discovered and identified for the first time.

A Preparative Method for the Isolation of Calponin from Molluscan Catch Muscle.

We describe the development of a preparative method to isolate molluscan catch muscle, calponin. This method is based on the ability of calponin to interact with actin in a temperature-dependent manner. After extracting thin filaments, as previously described, the extract was ultracentrifuged at 2 °C.

Modeling of the mussel catch muscle contractile apparatus in actomyosin suspension.

In this paper, we tried to create a contractile model from proteins of the catch muscle of the Gray mussel, similar to the well-described suspension contractile model of vertebrate skeletal muscles. This model makes it possible to characterize the processes in the reconstructed contractile apparatus with the help of monitoring the two characteristics of muscle suspensions - the optical density and the particle size. Contractile model of the catch muscle we constructed was the simplest model consisting of two proteins, actin and myosin.

Protein composition of thick filaments from molluscan catch muscle and the role of twitchin in the catch-state formation.

In the work, we performed densitometry of thick filaments of the Gray's mussel catch muscle; densitometry included determination of electrophoretic dye binding constants of proteins. The results of densitometry showed that the content of twitchin in thick filaments is significantly (10 times) lower than the content of myosin. We performed an in vitro simulation of the contractile apparatus of the catch muscle and showed that with such content, links formed by twitchin cannot stop "relaxation".

Non-Straub type actin from molluscan catch muscle.

We have developed a method of obtaining natural actin from smooth muscles of the bivalves on the example of the Сrenomytilus grayanus catch muscle. The muscles were previously rigorized to prevent a loss of thin filaments during homogenization and washings. Thin filaments were isolated with a low ionic strength solution in the presence of ATP and sodium pyrophosphate.

Troponin-like regulation in muscle thin filaments of the mussel Crenomytilus grayanus (Bivalvia: Mytiloida).

Muscles of bivalve molluscs have double calcium regulation--myosin-linked and actin-linked. While the mechanism of myosin-linked regulation is sufficiently studied, there is still no consensus on the mechanism of actin-linked regulation. Earlier we showed a high degree of Ca2+-sensitivity of thin filaments from the adductor muscle of the mussel Crenomytilus grayanus (Mytiloida).

Hybrid and non-hybrid actomyosins reconstituted with actin, myosin and tropomyosin from skeletal and catch muscles.

In this study, we investigated hybrid and non-hybrid actomyosin models including key contractile proteins: actin, myosin, and tropomyosin. These proteins were isolated from the rabbit skeletal muscle and the catch muscle of the mussel Crenomytilus grayanus. Our results confirmed literature data on an unusual ability of bivalve's tropomyosin to inhibit Mg-ATPase activity of skeletal muscle actomyosin.

Molluscan smooth catch muscle contains calponin but not caldesmon.

We isolated Ca(2+)-regulated thin filaments from the smooth muscle of the mussel Crenomytilus grayanus and studied the protein composition of different preparations from this muscle: whole muscle, heat-stable extract, fractions from heat-stable extract, thin filaments and intermediate stages of thin filaments purification. Among the protein components of the above-listed preparations, we did not find caldesmon (CaD), although two isoforms of a calponin-like (CaP-like) protein, which along with CaD is characteristic of vertebrate smooth muscle, were present in thin filaments. Thus, CaD is not Ca(2+)-regulator of thin filaments of this muscle.