Purification of human muscle satellite cells by flow cytometry

Baroffio, Anne; Aubry, Jean‐Pierre; Kaelin, André; Krause, Ryoko; Hamann, Martine; Bader, Charles

doi:10.1002/mus.880160511

Cited by 68 publications

(79 citation statements)

References 20 publications

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“…Thus, desmin appears to be a marker of post-embryonic striated muscle cells irrespective of their stage of differentiation, except for bovine and some avian muscle precursor cells (Grounds, 1991). NCAM, in contrast, is rarely detectable in quiescent satellite cells (at least in mouse and rat, this study and Grounds, 1991) and present only in a (more mature) fraction of the myoblasts (Baroffio et al, 1993;MacCalman et al, 1992; this paper, and un- published observations). NCAM persists at later stages (myotubes and muscle fibers) until functional innervation is acquired (Covault and Sanes, 1986;Cashman et al, 1987;Wernig et al, 1991;Irintchev et al, 1993).…”

Section: Regenerating Musclesmentioning

confidence: 49%

Expression pattern of M‐cadherin in normal, denervated, and regenerating mouse muscles

Irintchev

Zeschnigk

Starzinski‐Powitz

et al. 1994

Developmental Dynamics

318

266

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Section: Regenerating Musclesmentioning

confidence: 49%

Expression pattern of M‐cadherin in normal, denervated, and regenerating mouse muscles

Irintchev

Zeschnigk

Starzinski‐Powitz

et al. 1994

Developmental Dynamics

318

266

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“…Cell Culture-Muscle samples, cell dissociation, and clonal culture from satellite cells were prepared as previously described (33,47). Human muscle samples were obtained from eight children (operated for clubfoot and less than 4 years old) without any known neuromuscular disease.…”

Section: Methodsmentioning

confidence: 99%

Human Muscle Economy Myoblast Differentiation and Excitation-Contraction Coupling Use the Same Molecular Partners, STIM1 and STIM2

Darbellay

Arnaudeau

Ceroni

et al. 2010

Journal of Biological Chemistry

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Our recent work identified store-operated Ca 2؉ entry (SOCE) as the critical Ca 2؉ source required for the induction of human myoblast differentiation (Darbellay, B., Arnaudeau, S., König, S., Jousset, H., Bader, C., Demaurex, N., and Bernheim, L. (2009) J. Biol. Chem. 284, 5370 -5380). The present work indicates that STIM2 silencing, similar to STIM1 silencing, reduces myoblast SOCE amplitude and differentiation. Because myoblasts in culture can be induced to differentiate into myotubes, which spontaneously contract in culture, we used the same molecular tools to explore whether the Ca 2؉ mechanism of excitation-contraction coupling also relies on STIM1 and STIM2. Live cell imaging of early differentiating myoblasts revealed a characteristic clustering of activated STIM1 and STIM2 during the first few hours of differentiation. Thapsigargin-induced depletion of endoplasmic reticulum Ca 2؉ content caused STIM1 and STIM2 redistribution into clusters, and co-localization of both STIM proteins. Interaction of STIM1 and STIM2 was revealed by a rapid increase in fluorescence resonance energy transfer between CFP-STIM1 and YFP-STIM2 after SOCE activation and confirmed by co-immunoprecipitation of endogenous STIM1 and STIM2. Although both STIM proteins clearly contribute to SOCE and are required during the differentiation process, STIM1 and STIM2 are functionally largely redundant as overexpression of either STIM1 or STIM2 corrected most of the impact of STIM2 or STIM1 silencing on SOCE and differentiation. With respect to excitation-contraction, we observed that human myotubes rely also on STIM1 and STIM2 to refill their endoplasmic reticulum Ca 2؉ -content during repeated KCl-induced Ca 2؉ releases. This indicates that STIM2 is a necessary partner of STIM1 for excitation-contraction coupling. Thus, both STIM proteins are required and interact to control SOCE during human myoblast differentiation and human myotube excitationcontraction coupling. STIM1 and STIM2 are endoplasmic reticulum (ER)2 transmembrane proteins that are activated by a drop in Ca 2ϩ content in the ER (2-5). Once activated, STIM1 and STIM2 trigger a Ca 2ϩ influx (also called store-operated Ca 2ϩ entry (SOCE)) through Ca 2ϩ -selective Orai channels located at the plasma membrane (6 -13). This Ca 2ϩ influx restores the ER Ca 2ϩ content (2-4, 10, 12, 14 -26).Several studies examined whether STIM2 had a specific role, distinct from STIM1, but no clear answer has emerged yet. A lower Ca 2ϩ -activation threshold of STIM2 as compared with STIM1 has been suggested (2), although N-terminal Ca 2ϩ -binding affinity seems to be similar for STIM1 and STIM2 (27-29). In STIM2 knock-out mice, and also in several cell types in which STIM2 has been silenced, SOCE amplitude is only slightly reduced. This could reflect either a smaller activation of Orai1 by the N-terminal part of STIM2 or a lower expression of STIM2 as compared with STIM1 (3,4,24,30). In other studies, overexpression of STIM2 has been reported to inhibit SOCE (31) or, on the contrary, to restore SOCE i...

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“…Human mpc were cultured from muscle samples as described previously, in Ham's-F12 medium containing 15% fetal calf serum (FCS) (growth medium, GM) and antibiotics (Authier et al, 1999). Human mpc seeded at 5000 cells/ cm 2 undergo proliferation and at day 4 of culture (nearly confluence), the medium was replaced with Ham's-F12 medium containing 5% FCS (differentiation medium, DM) to induce myogenic differentiation characterized by mpc fusion into myotubes (Baroffio et al, 1993). By using this procedure, mpc undergo standardized myogenic differentiation, including proliferation phase up to day 4, and then withdrawal of cell cycle to enter differentiation and formation of small myotubes (day 7), and growth of preformed myotubes through accretion of additional mpc (day 14).…”

Section: Cell Culturementioning

confidence: 99%

ADAM12 and α₉β₁Integrin Are Instrumental in Human Myogenic Cell Differentiation

Lafuste

Sonnet

Chazaud

et al. 2005

MBoC

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Knowledge on molecular systems involved in myogenic precursor cell (mpc) fusion into myotubes is fragmentary. Previous studies have implicated the a disintegrin and metalloproteinase (ADAM) family in most mammalian cell fusion processes. ADAM12 is likely involved in fusion of murine mpc and human rhabdomyosarcoma cells, but it requires yet unknown molecular partners to launch myogenic cell fusion. ADAM12 was shown able to mediate cell-to-cell attachment through binding ␣ 9 ␤ 1 integrin. We report that normal human mpc express both ADAM12 and ␣ 9 ␤ 1 integrin during their differentiation. Expression of ␣ 9 parallels that of ADAM12 and culminates at time of fusion. ␣ 9 and ADAM12 coimmunoprecipitate and participate to mpc adhesion. Inhibition of ADAM12/␣ 9 ␤ 1 integrin interplay, by either ADAM12 antisense oligonucleotides or blocking antibody to ␣ 9 ␤ 1 , inhibited overall mpc fusion by 47-48%, with combination of both strategies increasing inhibition up to 62%. By contrast with blockade of vascular cell adhesion molecule-1/␣ 4 ␤ 1 , which also reduced fusion, exposure to ADAM12 antisense oligonucleotides or anti-␣ 9 ␤ 1 antibody did not induce detachment of mpc from extracellular matrix, suggesting specific involvement of ADAM12-␣ 9 ␤ 1 interaction in the fusion process. Evaluation of the fusion rate with regard to the size of myotubes showed that both ADAM12 antisense oligonucleotides and ␣ 9 ␤ 1 blockade inhibited more importantly formation of large (>5 nuclei) myotubes than that of small (2-4 nuclei) myotubes. We conclude that both ADAM12 and ␣ 9 ␤ 1 integrin are expressed during postnatal human myogenic differentiation and that their interaction is mainly operative in nascent myotube growth. INTRODUCTIONAdult skeletal muscle regeneration after injury results from activation, proliferation, and fusion of mononucleated myogenic precursor cells (mpc) (Hawke and Garry, 2001). The mpc fusion results from an ordered sequence of events, including clustering and alignment of cells, establishment of close cell-to-cell contacts, and plasma membrane merging (Doberstein et al., 1997;Taylor, 2003). Various membrane proteins have been implicated in myotube formation, including N-and M-cadherins, neural cell adhesion molecule (NCAM), and vascular cell adhesion molecule (VCAM), ␣ 4 ␤ 1 and other integrins, and a disintegrin and metalloproteinases (ADAMs) (Abmayr et al., 2003). ADAMs form a family of Ͼ30 transmembrane glycoproteins with a unique domain organization, including a prodomain, a proteolytic domain (metalloprotease), an adhesion integrin-binding site formed by both disintegrin and cysteine-rich domains, an epidermal growth factor-like domain, a transmembrane domain, and a signaling cytoplasmic tail (Huovila et al., 1996;Primakoff and Myles, 2002;White, 2003). In addition, some ADAMs contain a hydrophobic sequence in a cysteine-rich region that may represent a fusion peptide, suggesting that this subclass of ADAMs might participate to plasma membrane merging (Huovila et al., 1996). Some ADAMs have been implicated i...

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Purification of human muscle satellite cells by flow cytometry

Cited by 68 publications

References 20 publications

Expression pattern of M‐cadherin in normal, denervated, and regenerating mouse muscles

Expression pattern of M‐cadherin in normal, denervated, and regenerating mouse muscles

Human Muscle Economy Myoblast Differentiation and Excitation-Contraction Coupling Use the Same Molecular Partners, STIM1 and STIM2

ADAM12 and α₉β₁Integrin Are Instrumental in Human Myogenic Cell Differentiation

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Purification of human muscle satellite cells by flow cytometry

Cited by 68 publications

References 20 publications

Expression pattern of M‐cadherin in normal, denervated, and regenerating mouse muscles

Expression pattern of M‐cadherin in normal, denervated, and regenerating mouse muscles

Human Muscle Economy Myoblast Differentiation and Excitation-Contraction Coupling Use the Same Molecular Partners, STIM1 and STIM2

ADAM12 and α9β1Integrin Are Instrumental in Human Myogenic Cell Differentiation

Contact Info

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ADAM12 and α₉β₁Integrin Are Instrumental in Human Myogenic Cell Differentiation