An emilin family extracellular matrix protein identified in the cochlear basilar membrane

Amma, Lori L.; Goodyear, Richard J.; Faris, Jonathan S.; Jones, Iwan; Ng, Lily; Richardson, Guy P.; Forrest, Douglas

doi:10.1016/s1044-7431(03)00075-7

Cited by 35 publications

(32 citation statements)

References 47 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Levels of Emilin-2 increase within the BM between postnatal days 1e13 and are dependent on thyroid hormone (Amma et al, 2003). Based on these results it has been suggested that Emilin2 could play a role in the assembly or elasticity of the BM during development (Amma et al, 2003). This hypothesis is supported by the observation that the development of the passive mechanical properties of the BM are delayed in hypothyroid mice (Anniko and Rosenkvist, 1982;Song et al, 2008), suggesting a potentially broader role for thyroid hormone in BM development.…”

Section: Characteristics Of the Basilar Membranementioning

confidence: 83%

“…More recently, Emilin2, a member of a family of glycoproteins that have been implicated in extracellular elasticity, has also been localized to the BM. Levels of Emilin-2 increase within the BM between postnatal days 1e13 and are dependent on thyroid hormone (Amma et al, 2003). Based on these results it has been suggested that Emilin2 could play a role in the assembly or elasticity of the BM during development (Amma et al, 2003).…”

Section: Characteristics Of the Basilar Membranementioning

confidence: 88%

See 1 more Smart Citation

Development of tonotopy in the auditory periphery

Mann

Kelley

2011

Hearing Research

View full text Add to dashboard Cite

Section: Characteristics Of the Basilar Membranementioning

confidence: 83%

Section: Characteristics Of the Basilar Membranementioning

confidence: 88%

Development of tonotopy in the auditory periphery

Mann

Kelley

2011

Hearing Research

View full text Add to dashboard Cite

“…Also known as mesothelial cells, TBCs were first described in mammals by Claudius (Claudius, 1856), and subsequently in more detail in other species, including humans (Bhatt et al, 2001;Cabezudo, 1978;Keithley et al, 1994). Because of their close association with the basilar membrane, TBCs have been suggested to secrete extracellular matrix proteins (Amma et al, 2003). Others have proposed a biomechanical role for the TBCs, as their number varies along the cat cochlea (Cabezudo, 1978).…”

Section: Discussionmentioning

confidence: 99%

Tympanic border cells are Wnt-responsive and can act as progenitors for postnatal mouse cochlear cells

et al. 2013

View full text Add to dashboard Cite

SUMMARYPermanent hearing loss is caused by the irreversible damage of cochlear sensory hair cells and nonsensory supporting cells. In the postnatal cochlea, the sensory epithelium is terminally differentiated, whereas tympanic border cells (TBCs) beneath the sensory epithelium are proliferative. The functions of TBCs are poorly characterized. Using an Axin2 lacZ Wnt reporter mouse, we found transient but robust Wnt signaling and proliferation in TBCs during the first 3 postnatal weeks, when the number of TBCs decreases. In vivo lineage tracing shows that a subset of hair cells and supporting cells is derived postnatally from Axin2-expressing TBCs. In cochlear explants, Wnt agonists stimulated the proliferation of TBCs, whereas Wnt inhibitors suppressed it. In addition, purified Axin2 lacZ cells were clonogenic and self-renewing in culture in a Wnt-dependent manner, and were able to differentiate into hair celllike and supporting cell-like cells. Taken together, our data indicate that Axin2-positive TBCs are Wnt responsive and can act as precursors to sensory epithelial cells in the postnatal cochlea.

show abstract

“…Apart from MMRN1 that is deposited in the ECM but for the most part is sequestered in megakaryocytes, endothelial cells (ECs), and platelets granules (Adam et al, 2005), the members of the EMILIN family are constituents of the ECM Under normal conditions the expression of each individual gene overlaps with those of some other members of the family; the only exception is apparently the central nervous system, where only EMILIN2 is detected outside blood vessels, at least at the mRNA level (Braghetta et al, 2004). Moreover, EMILIN2 is specifically and abundantly expressed in mouse cochlear basilar membrane (Amma et al, 2003). …”

Section: The Emilin/multimerin Family Of Proteinsmentioning

confidence: 99%

The EMILIN/Multimerin Family

Colombatti¹,

Spessotto²,

Doliana³

et al. 2012

Front. Immun.

View full text Add to dashboard Cite

Elastin microfibrillar interface proteins (EMILINs) and Multimerins (EMILIN1, EMILIN2, Multimerin1, and Multimerin2) constitute a four member family that in addition to the shared C-terminus gC1q domain typical of the gC1q/TNF superfamily members contain a N-terminus unique cysteine-rich EMI domain. These glycoproteins are homotrimeric and assemble into high molecular weight multimers. They are predominantly expressed in the extracellular matrix and contribute to several cellular functions in part associated with the gC1q domain and in part not yet assigned nor linked to other specific regions of the sequence. Among the latter is the control of arterial blood pressure, the inhibition of Bacillus anthracis cell cytotoxicity, the promotion of cell death, the proangiogenic function, and a role in platelet hemostasis. The focus of this review is to highlight the multiplicity of functions and domains of the EMILIN/Multimerin family with a particular emphasis on the regulatory role played by the ligand–receptor interactions of the gC1q domain. EMILIN1 is the most extensively studied member both from the structural and functional point of view. The structure of the gC1q of EMILIN1 solved by NMR highlights unique characteristics compared to other gC1q domains: it shows a marked decrease of the contact surface of the trimeric assembly and while conserving the jelly-roll topology with two β-sheets of antiparallel strands it presents a nine-stranded β-sandwich fold instead of the usual 10-stranded fold. This is likely due to the insertion of nine residues that disrupt the ordered strand organization and forma a highly dynamic protruding loop. In this loop the residue E933 is the site of interaction between gC1q and the α4β1 and α9β1 integrins, and contrary to integrin occupancy that usually upregulates cell growth, when gC1q is ligated by the integrin the cells reduce their proliferative activity.

show abstract

An emilin family extracellular matrix protein identified in the cochlear basilar membrane

Cited by 35 publications

References 47 publications

Development of tonotopy in the auditory periphery

Development of tonotopy in the auditory periphery

Tympanic border cells are Wnt-responsive and can act as progenitors for postnatal mouse cochlear cells

The EMILIN/Multimerin Family

Contact Info

Product

Resources

About