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The NH2-terminal peptide of alpha-smooth muscle actin inhibits force generation by the myofibroblast in vitro and in vivo.

ABSTRACT: Myofibroblasts are specialized fibroblasts responsible for granulation tissue contraction and the soft tissue retractions occurring during fibrocontractive diseases. The marker of fibroblast-myofibroblast modulation is the neo expression of alpha-smooth muscle actin (alpha-SMA), the actin isoform typical of vascular smooth muscle cells that has been suggested to play an important role in myofibroblast force generation. Actin isoforms differ slightly in their NH2-terminal sequences; these conserved differences suggest different functions. When the NH2-terminal sequence of alpha-SMA Ac-EEED is delivered to cultured myofibroblast in the form of a fusion peptide (FP) with a cell penetrating sequence, it inhibits their contractile activity; moreover, upon topical administration in vivo it inhibits the contraction of rat wound granulation tissue. The NH2-terminal peptide of alpha-skeletal actin has no effect on myofibroblasts, whereas the NH2-terminal peptide of beta-cytoplasmic actin abolishes the immunofluorescence staining for this isoform without influencing alpha-SMA distribution and cell contraction. The FPs represent a new tool to better understand the specific functions of actin isoforms. Our findings support the crucial role of alpha-SMA in wound contraction. The alpha-SMA-FP will be useful for the understanding of the mechanisms of connective tissue remodeling; moreover, it furnishes the basis for a cytoskeleton-dependent preventive and/or therapeutic strategy for fibrocontractive pathological situations.

SUBMITTER: Hinz B

PROVIDER: S-EPMC2173846 | biostudies-other | 2002 May

REPOSITORIES: biostudies-other

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The NH2-terminal peptide of alpha-smooth muscle actin inhibits force generation by the myofibroblast in vitro and in vivo.

Hinz Boris B Gabbiani Giulio G Chaponnier Christine C

The Journal of cell biology 20020506 4

Myofibroblasts are specialized fibroblasts responsible for granulation tissue contraction and the soft tissue retractions occurring during fibrocontractive diseases. The marker of fibroblast-myofibroblast modulation is the neo expression of alpha-smooth muscle actin (alpha-SMA), the actin isoform typical of vascular smooth muscle cells that has been suggested to play an important role in myofibroblast force generation. Actin isoforms differ slightly in their NH2-terminal sequences; these conserv ...[more]

PMID: 11994316

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Project description:The stomach serves as food reservoir, mixing organ and absorption area for certain substances, while continually varying its position and size. Large dimensional changes during ingestion and gastric emptying of the stomach are associated with large changes in smooth muscle length. These length changes might induce history-effects, namely force depression (FD) following active muscle shortening and force enhancement (FE) following active muscle stretch. Both effects have impact on the force generating capacity of the stomach, and thus functional relevance. However, less is known about history-effects and active smooth muscle properties of stomach smooth muscle. Thus, the aim of this study was to investigate biomechanical muscle properties as force-length and force-velocity relations (FVR) of porcine stomach smooth muscle strips, extended by the analysis of history-effects on smooth muscle force. Therefore, in total n = 54 tissue strips were dissected in longitudinal direction from the ventral fundus of porcine stomachs. Different isometric, isotonic, and isokinetic contraction protocols were performed during electrical muscle stimulation. Cross-sectional areas (CSA) of smooth muscles were determined from cryo-histological sections stained with Picrosirius Red. Results revealed that maximum smooth muscle tension was 10.4 ± 2.6 N/cm2. Maximum shortening velocity (Vmax ) and curvature factor (curv) of the FVR were 0.04 ± 0.01 [optimum muscle length/s] and 0.36 ± 0.15, respectively. The findings of the present study demonstrated significant (P < 0.05) FD [up to 32% maximum muscle force (Fim )] and FE (up to 16% Fim ) of gastric muscle tissue, respectively. The FE- and FD-values increased with increasing ramp amplitude. This outstanding muscle behavior is not accounted for in existing models so far and strongly supports the idea of a holistic reflection of distinct stomach structure and function. For the first time this study provides a comprehensive set of stomach smooth muscle parameters including classic biomechanical muscle properties and history-dependent effects, offering the possibility for the development and validation of computational stomach models. Furthermore, this data set facilitates novel insights in gastric motility and contraction behavior based on the re-evaluation of existing contractile mechanisms. That will likely help to understand physiological functions or dysfunctions in terms of gastric accommodation and emptying.

Dataset Information

The NH2-terminal peptide of alpha-smooth muscle actin inhibits force generation by the myofibroblast in vitro and in vivo.

Publications

The NH2-terminal peptide of alpha-smooth muscle actin inhibits force generation by the myofibroblast in vitro and in vivo.

Similar Datasets

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