Last update 01 Nov 2024

MYH2

Last update 01 Nov 2024

Basic Info

Synonyms

IBM3, MYH2, MYH2A

+ [9]

Introduction

Muscle contraction. Required for cytoskeleton organization (By similarity).

Drugs associated with MYH2

MTR-601

Target

MYH2

Mechanism

MYH2 inhibitors

Active Org.

Motric Bio

Originator Org.

Motric Bio

Active Indication

Cerebral Palsy [+6]

Inactive Indication-

Drug Highest PhasePhase 1

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

MPH-220

Target

MYH2

Mechanism

MYH2 inhibitors

Active Org.

MyoKardia, Inc. [+3]

Originator Org.

Motorpharma Ltd.Startup

Active Indication

Muscle Spasticity

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

Blebbistatin

Target

Cardiac myosin x MYH2

Mechanism

Cardiac myosin inhibitors [+1]

Active Org.

Harvard Medical School

Originator Org.

Harvard Medical School

Active Indication-

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

Clinical Trials associated with MYH2

NCT06117020 / RecruitingPhase 1

A Randomized, Double-Blind, Placebo-Controlled, First-in-Human, Single and Multiple Ascending Dose Study of MTR-601 in Healthy Volunteers.

To assess the safety and tolerability of single and multiple doses of MTR-601 in normal healthy volunteers under fed and fasted conditions.
To evaluate the plasma and urine pharmacokinetics (PK) of MTR-601. To evaluate the pharmacodynamic (PD) effects of MTR-601 on muscle strength and muscle accumulation of MTR-601 by muscle biopsy and other potential mechanistic, predictive and PD markers of MTR-601.

Start Date11 Sep 2023

Sponsor / Collaborator

Motric Bio

100 Clinical Results associated with MYH2

100 Translational Medicine associated with MYH2

0 Patents (Medical) associated with MYH2

947

Literatures (Medical) associated with MYH2

01 Dec 2024·Cellular and Molecular Life Sciences

Structure, regulation, and mechanisms of nonmuscle myosin-2

Review

Author: Heissler, Sarah M ; Chinthalapudi, Krishna

AbstractMembers of the myosin superfamily of molecular motors are large mechanochemical ATPases that are implicated in an ever-expanding array of cellular functions. This review focuses on mammalian nonmuscle myosin-2 (NM2) paralogs, ubiquitous members of the myosin-2 family of filament-forming motors. Through the conversion of chemical energy into mechanical work, NM2 paralogs remodel and shape cells and tissues. This process is tightly controlled in time and space by numerous synergetic regulation mechanisms to meet cellular demands. We review how recent advances in structural biology together with elegant biophysical and cell biological approaches have contributed to our understanding of the shared and unique mechanisms of NM2 paralogs as they relate to their kinetics, regulation, assembly, and cellular function.

01 Nov 2024·The Journal of Immunology

Chitinase 3–like-1 Inhibits Innate Antitumor and Tissue Remodeling Immune Responses by Regulating CD47-SIRPα– and CD24-Siglec10–Mediated Phagocytosis

Article

Author: Choi, Augustine M. K. ; Yee, Daniel C. ; Zhu, Zhou ; Lee, Joyce H. ; Lee, Chun Geun ; Elias, Jack A. ; Kamle, Suchitra ; Lee, Chang-Min ; Silverman, Edwin K. ; Ma, Bing ; Sadanaga, Takayuki ; DeMeo, Dawn L.

AbstractInnate immune responses such as phagocytosis are critically linked to the generation of adaptive immune responses against the neoantigens in cancer and the efferocytosis that is essential for homeostasis in diseases characterized by lung injury, inflammation, and remodeling as in chronic obstructive pulmonary disease (COPD). Chitinase 3–like-1 (CHI3L1) is induced in many cancers where it inhibits adaptive immune responses by stimulating immune checkpoint molecules (ICPs) and portends a poor prognosis. CHI3L1 is also induced in COPD where it regulates epithelial cell death. In this study, we demonstrate that pulmonary melanoma metastasis inhibits macrophage phagocytosis by stimulating the CD47-SIRPα and CD24-Siglec10 phagocytosis checkpoint pathways while inhibiting macrophage “eat me” signals from calreticulin and HMGB1. We also demonstrate that these effects on macrophage phagocytosis are associated with CHI3L1 stimulation of the SHP-1 and SHP-2 phosphatases and inhibition of the accumulation and phosphorylation of cytoskeleton-regulating nonmuscle myosin IIa. This inhibition of innate immune responses such as phagocytosis provides a mechanistic explanation for the ability of CHI3L1 to stimulate ICPs and inhibit adaptive immune responses in cancer and diseases such as COPD. The ability of CHI3L1 to simultaneously inhibit innate immune responses, stimulate ICPs, inhibit T cell costimulation, and regulate a number of other oncogenic and inflammation pathways suggests that CHI3L1-targeted therapeutics are promising interventions in cancer, COPD, and other disorders.

01 Oct 2024·Food Chemistry

Comparative analysis of the longissimus muscle proteome of European wild boar and domestic pig in response to thermal processing

Article

Author: Fornal, Emilia ; Kasałka-Czarna, Natalia ; Montowska, Magdalena ; Sumara, Agata

This study tries to fill the knowledge gap regarding differences in the expression of proteins in the meat of European wild boar (Sus scrofa scrofa) and domestic pig (Sus scrofa domestica), considering the impact of thermally induced degradation. We assessed relative protein changes between cooked longissimus thoracis et lumborum (LTL) muscle proteomes by using mass spectrometry, chemometric, label-free proteomic, and bioinformatic tools. Among 30 differentially abundant proteins identified MyHC-2a, ATPs-α, CK-S, ADP/ATPt1, IDH2, and MyBP-C1 were upregulated (x > 1) whereas NEB, γ-ENO and EPSF were downregulated (x < 1) in wild boar. ShinyGO and KEGG database pathway analyses revealed that these proteins are mainly involved in processes related to muscle contraction and various pathways of glucose metabolism and energy production. Protein expression changes could have been caused by the different muscle activity of wild animals in response to prolonged movement associated with foraging for food in the natural environment.

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MYH2

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