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Introduction: α7β1 integrin links the extracellular matrix to the focal adhesion (FA) in skeletal muscle and serves as a stabilizing and signal relayer. Heat shock (HS) induces expression of proteins that interact with the FA.
Methods: Male Wistar rats were assigned to 1 of 3 groups: control (CON); eccentric exercise (EE); or EE+HS (HS). Soleus muscle was analyzed at 2 h and 48 h post-exercise.
Results: The 120-kDa α7 integrin decreased in the EE and HS groups, and the 70-kDa peptide decreased in the EE group at 2 h post-exercise. Total expression of focal adhesion kinase (FAK) and RhoA were decreased in EE and HS at 2 h post-exercise. Expression of phosphorylated FAK(397) decreased in the EE group but not the HS group at 2 h post-exercise.
Conclusions: Long-duration EE may cause alterations in the FA in rat soleus muscle through the α7 integrin subunit and FAK.
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http://dx.doi.org/10.1002/mus.24324 | DOI Listing |
J Anat
September 2025
Department of Anatomy and Cell Biology, Hyogo Medical University School of Medicine, Nishinomiya, Hyogo, Japan.
The white matter of the spinal cord is essential for sensory and motor signaling, and its proper development is crucial for establishing functional neuronal circuits. However, the mechanisms underlying white matter formation remain incompletely understood. We hypothesized that the extracellular matrix, particularly laminins, plays a key role in this process.
View Article and Find Full Text PDFBiochim Biophys Acta Rev Cancer
September 2025
Integrated Traditional Chinese and Western Medicine In Proctology, The First Affiliated Hospital, College of Clinical Medicine of Henan University of Science and Technology, Luoyang 471003, Henan Province, China. Electronic address:
Glycosylation, a pivotal post-translational modification, critically influences colorectal cancer (CRC) progression via dysregulated N- and O-linked pathways, characterized by oligomannose, fucosylation, hypersialylation, truncated O-glycans (Tn, sialyl-Tn), branched N-glycans, and Lewis antigens. These alterations promote tumor aggressiveness, immune evasion, and metastasis through glycoprotein remodeling (e.g.
View Article and Find Full Text PDFImmunity
September 2025
Key Laboratory of Multi-cell Systems, CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, University of Chinese Academy of Sciences, Chinese Academy of Sciences, Shanghai, China. Electronic address:
In this issue of Immunity, Lv et al. develop a new CAR-T cell culture system that uses integrin mechanical signaling to boost CAR-T proliferation while preserving stemness, pointing out a new direction of CAR-T manufacturing.
View Article and Find Full Text PDFThromb Res
September 2025
Departamento de Química and Institute for advanced research in chemical Science (IAdChem), Facultad de Ciencias, Módulo 13, Universidad Autónoma de Madrid, 28049, Madrid, Spain.
Platelet integrin αIIbβ3 is the final common effector of arterial thrombosis: it switches from a low-affinity to a high-affinity state, binds fibrinogen, and initiates the outside-in signals that stabilize a growing clot. Calcium- and integrin-binding protein 1 (CIB1) emerged as the first endogenous partner of the αIIb cytoplasmic tail and is now recognized as a dual-role adaptor. At rest, Ca-free CIB1 tethers the inner membrane clasp and restrains premature integrin activation; after ligand engagement, Ca-bound CIB1 docks onto αIIb, recruits focal-adhesion kinase and amplifies Src-dependent cytoskeletal remodeling.
View Article and Find Full Text PDFSci Adv
September 2025
Division of Basic Sciences, Fred Hutchinson Cancer Center, Seattle, WA 98109, USA.
Integrins bind ligands between their alpha (α) and beta (β) subunits and transmit signals through conformational changes. Early in chordate evolution, some α subunits acquired an "inserted" (I) domain that expanded integrin's ligand-binding repertoire but obstructed the ancestral ligand pocket, seemingly blocking conventional integrin activation. Here, we compare cryo-electron microscopy structures of apo and ligand-bound states of the I domain-containing αEβ integrin and the I domain-lacking αβ integrin to illuminate how the I domain intrinsically mimics an extrinsic ligand to preserve integrin function.
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