Cadherin

Cadherins (named for "calcium-dependent

adhesion") are a type of cell adhesion molecule
(CAM) that is important in the formation of
adherens junctions to bind cells with each
other.[1] Cadherins are a class of type-1
transmembrane proteins. They are dependent on
calcium (Ca2+) ions to function, hence their
name. Cell-cell adhesion is mediated by
extracellular cadherin domains, whereas the
intracellular cytoplasmic tail associates with
numerous adaptor and signaling proteins,
collectively referred to as the cadherin adhesome.

The cadherin superfamily includes cadherins,

protocadherins, desmogleins, and desmocollins,
and more.[2][3] In structure, they share cadherin
repeats, which are the extracellular Ca2+-binding
domains. There are multiple classes of cadherin
molecule, each designated with a prefix (in
general, noting the type of tissue with which it is
associated). It has been observed that cells
containing a specific cadherin subtype tend to
cluster together to the exclusion of other types, Principal interactions of structural proteins at cadherin-
both in cell culture and during development. [4] based adherens junction. Actin filaments are linked to α-
For example, cells containing N-cadherin tend to actinin and to membrane through vinculin. The head domain
of vinculin associates to E-cadherin via α-, β-, and γ-
cluster with other N-cadherin-expressing cells.
catenins. The tail domain of vinculin binds to membrane
However, it has been noted that the mixing speed
lipids and to actin filaments.
in the cell culture experiments can have an effect
on the extent of homotypic specificity.[5] In
addition, several groups have observed
heterotypic binding affinity (i.e., binding of different types of cadherin together) in various assays.[6][7] One
current model proposes that cells distinguish cadherin subtypes based on kinetic specificity rather than
thermodynamic specificity, as different types of cadherin homotypic bonds have different lifetimes.[8]

Contents
Structure
Function
Development
Tumour metastasis
Correlation to cancer
Correlation to endometrium and embryogenesis
Types
Classical
 Desmosomal
Protocadherins
Unconventional/ungrouped
See also
References
Further reading
External links

Structure
Cadherins are synthesized as polypeptides and undergo many post-
translational modifications to become the proteins which mediate cell-
cell adhesion and recognition.[9] These polypeptides are
approximately 720–750 amino acids long. Each cadherin has a small
C-terminal cytoplasmic component, a transmembrane component, and
the remaining bulk of the protein is extra-cellular (outside the cell).
The transmembrane component consists of single chain glycoprotein
repeats.[10] Because cadherins are Ca2+ dependent, they have five
tandem extracellular domain repeats that act as the binding site for
Ca2+ ions.[11] Their extracellular domain interacts in two
separate trans dimer conformations: strand-swap dimers (S-dimers)
and X-dimers.[11] To date, over 100 types of cadherins in humans
have been identified and sequenced.[12] Domain organization of different
types of cadherins
The functionality of cadherins relies upon the formation of two
identical subunits, known as homodimers.[10] The homodimeric
cadherins create cell-cell adhesion with cadherins present in the membranes of other cells through changing
conformation from cis-dimers to trans-dimers.[10] Once the cell-cell adhesion between cadherins present in the
cell membranes of two different cells has formed, adherens junctions can then be made when protein
complexes, usually composed of α-, β-, and γ-catenins, bind to the cytoplasmic portion of the cadherin.[10]

Function

Development

Cadherins behave as both receptors and ligands for other molecules. During development, their behavior
assists in properly positioning cells: they are responsible for the separation of the different tissue layers, and for
cellular migration.[13] In the very early stages of development, E-cadherin (epithelial cadherin) is most greatly
expressed. Many cadherins are specified for specific functions in the cell, and they are differentially expressed
in a developing embryo. For example, during neurulation, when the neural plate is forming in the embryo, the
tissues residing near the cranial neural folds have decreased N-cadherin expression.[14] Conversely, the
expression of the N-cadherins remains unchanged in the other regions of the neural tube that is located on the
anterior-posterior axis of the vertebrate.[14] The expression of the different types of cadherins in the cell are
varying dependent upon the specific differentiation and specification of the organism during development.
Cadherins play a vital role in the migration of cells through the epithelial-mesenchymal transition (EMT),
which requires cadherins to form adherents junctions with neighboring cells. In neural crest cells, which are
transient cells that arise in the developing organism during gastrulation and function in the patterning of the
vertebrate body plan, the cadherins are necessary to allow migration of cells to form tissues or organs.[14] In
addition, cadherins responsible in the EMT event in early development have also been shown to be critical in
the reprogramming of specified adult cells into a pluripotent state, forming induced pluripotent stem cells
(iPSCs).[1]

After development, cadherins play a role in maintaining cell and tissue structure, and in cellular movement.[12]
Regulation of cadherin expression can occur through promoter methylation among other epigenetic
mechanisms.[15]

Tumour metastasis

The E-cadherin–catenin complex plays a key role in cellular adhesion; loss of this function has been associated
with increased invasiveness and metastasis of tumors.[16] The suppression of E-cadherin expression is
regarded as one of the main molecular events responsible for dysfunction in cell-cell adhesion, which can lead
to local invasion and ultimately tumor development. Because of its important role tumor suppression, E-
cadherin is also referred to as the "suppressor of invasion".[17]

Correlation to cancer

It has been discovered that cadherins and other additional factors are correlated to the formation and growth of
some cancers and how a tumor continues to grow. The E-cadherins also known as the epithelial cadherins on
the surface of one cell can bind with those of the same kind on another to form bridges.[18] It is indicated that
the loss of the cell adhesion molecule E cadherin is causally involved in the formation of epithelial types of
cancers such as carcinomas. The changes in any type of cadherin expression may not only control tumor cell
adhesion but also affect signal transduction leading to the cancer cells growing uncontrollably.[19]

In epithelial cell cancers, disrupted cell to cell adhesion might lead to the development of secondary malignant
growths that are distant from the primary site of cancer, can result from the abnormalities in the expression of
E-cadherins or its associated catenins. CAMs such as the cadherin glycoproteins normally function as the glue
that holds cells together and act as important mediators of cell to cell interactions. E-cadherins, on the surface
of all epithelial cells, are linked to the actin cytoskeleton through interactions with catenins in the cytoplasm.
Thus, anchored to the cytoskeleton, E-cadherins on the surface of one cell can bind with those on another to
form bridges. In epithelial cell cancers, disrupted cell-cell adhesion that might lead to metastases can result
from abnormalities in the expression of E-cadherin or its associated catenins.[18]

Correlation to endometrium and embryogenesis

This family of glycoproteins are responsible for calcium-dependent mechanism of intracellular adhesion. E-
cadherins are crucial in embryogenesis during several processes, including gastrulation, neurulation and
organogenesis. Furthermore, suppression of E-cadherin impairs intracellular adhesion. The levels of this
molecule increases during the luteic phase, while its expression is regulated by progesterone with endometrial
calcitonin.[20]

Types
There are said to be over 100 different types of cadherins found in Cadherin domain (repeat)
vertebrates, which can be classified into four groups: classical,
desmosomal, protocadherins, and unconventional.[22][23] This large
amount of diversity is accomplished by having multiple cadherin
encoding genes combined with alternative RNA splicing
mechanisms. Invertebrates contain fewer than 20 types of
cadherins.[23]

Classical
Ribbon representation of a repeating
Different members of the cadherin family are found in different unit in the extracellular E-cadherin
locations. ectodomain of the mouse (PDB:
3Q2V (https://www.rcsb.org/structure/
CDH1 – E-cadherin (epithelial): E-cadherins are found in 3Q2V)) [21]
epithelial tissue; not to be confused with the APC/C
activator protein CDH1. Identifiers

CDH2 – N-cadherin (neural): N-cadherins are found in Symbol Cadherin

neurons Pfam PF00028 (http://pfa
CDH12 – cadherin 12, type 2 (N-cadherin 2) m.xfam.org/family?ac
CDH3 – P-cadherin (placental): P-cadherins are found in c=PF00028)
the placenta.
InterPro IPR002126 (https://w
ww.ebi.ac.uk/interpro/
Desmosomal entry/IPR002126)
SMART CA (http://smart.embl
Desmoglein (DSG1, DSG2, DSG3, DSG4)
-heidelberg.de/smart/
Desmocollin (DSC1, DSC2, DSC3)
do_annotation.pl?DO
MAIN=CA)
Protocadherins PROSITE PDOC00205 (http://w
ww.expasy.org/cgi-bi
Protocadherins are the largest mammalian subgroup of the cadherin n/prosite-search-ac?
superfamily of homophilic cell-adhesion proteins.
PDOC00205)
PCDH1 SCOPe 1nci (https://scop.ber
PCDH7 keley.edu/search/key
PCDH8 =1nci) / SUPFAM (htt
PCDH9 p://supfam.org/SUPE
PCDH10 RFAMILY/cgi-bin/sear
PCDH11X/11Y ch.cgi?search_field=1
PCDH12 nci)

PCDH15 Membranome 114 (http://membrano

PCDH17 me.org/protein_super
PCDH18 families/114)
PCDH19 Available protein structures:
PCDH20 Pfam structures (http://pfam.xfam.or
PCDHA1 g/family/PF00028?tab=pdbBlo
PCDHA2 ck) / ECOD (http://prodata.swm
ed.edu/ecod/complete/searc
PCDHA3 h?kw=PF00028)
PCDHA4 PDB RCSB PDB (http://www.rcsb.or
g/pdb/search/smartSubquery.d
PCDHA5
o?smartSearchSubtype=PfamI
PCDHA6 dQuery&pfamID=PF00028);
PCDHA7 PDBe (https://www.ebi.ac.uk/p
PCDHA8 dbe/entry/search/index?pfam_
PCDHA9 accession:PF00028); PDBj (htt
ps://pdbj.org/searchFor?query
PCDHA10
=PF00028)
PCDHA11
PDBsum structure summary (https://ww
PCDHA12 w.ebi.ac.uk/thornton-srv/datab
PCDHA13 ases/cgi-bin/pdbsum/GetPfam
PCDHAC1 Str.pl?pfam_id=PF00028)
PCDHAC2 See Pfam CL0159 (http://pfam.xfam.o
PCDHB1 rg/family/CL0159) for other Cadherin
PCDHB2 families.
PCDHB3
PCDHB4
PCDHB5
PCDHB6
PCDHB7
PCDHB8
PCDHB9
PCDHB10
PCDHB11
PCDHB12
PCDHB13
PCDHB14
PCDHB15
PCDHB16
PCDHB17
PCDHB18
PCDHGA1
PCDHGA2
PCDHGA3
PCDHGA4
PCDHGA5
PCDHGA6
PCDHGA7
PCDHGA8
PCDHGA9
PCDHGA10
PCDHGA11
PCDHGA12
PCDHGB1
PCDHGB2
PCDHGB3
 PCDHGB4
PCDHGB5
PCDHGB6
PCDHGB7
PCDHGC3
PCDHGC4
PCDHGC5
FAT
FAT2
FAT4

Unconventional/ungrouped
CDH4 – R-cadherin (retinal)
CDH5 – VE-cadherin (vascular endothelial)
CDH6 – K-cadherin (kidney)
CDH7 – cadherin 7, type 2
CDH8 – cadherin 8, type 2
CDH9 – cadherin 9, type 2 (T1-cadherin)
CDH10 – cadherin 10, type 2 (T2-cadherin)
CDH11 – OB-cadherin (osteoblast)
CDH13 – T-cadherin – H-cadherin (heart)
CDH15 – M-cadherin (myotubule)
CDH16 – KSP-cadherin
CDH17 – LI cadherin (liver-intestine)
CDH18 – cadherin 18, type 2
CDH19 – cadherin 19, type 2
CDH20 – cadherin 20, type 2
CDH23 – cadherin 23 (neurosensory epithelium)
CDH22, CDH24, CDH26, CDH28
CELSR1, CELSR2, CELSR3
CLSTN1, CLSTN2, CLSTN3
DCHS1, DCHS2,
LOC389118
PCLKC
RESDA1
RET

See also
Catenin
List of target antigens in pemphigus

References
 1. Alimperti S, Andreadis ST (May 2015). "CDH2 and CDH11 act as regulators of stem cell fate
decisions" (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4439315). Stem Cell Research. 14
(3): 270–82. doi:10.1016/j.scr.2015.02.002 (https://doi.org/10.1016%2Fj.scr.2015.02.002).
PMC 4439315 (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4439315). PMID 25771201 (http
s://pubmed.ncbi.nlm.nih.gov/25771201).
2. Hulpiau P, van Roy F (February 2009). "Molecular evolution of the cadherin superfamily". The
International Journal of Biochemistry & Cell Biology. 41 (2): 349–69.
doi:10.1016/j.biocel.2008.09.027 (https://doi.org/10.1016%2Fj.biocel.2008.09.027).
PMID 18848899 (https://pubmed.ncbi.nlm.nih.gov/18848899).
3. Angst BD, Marcozzi C, Magee AI (February 2001). "The cadherin superfamily: diversity in form
and function". Journal of Cell Science. 114 (Pt 4): 629–41. PMID 11171368 (https://pubmed.nc
bi.nlm.nih.gov/11171368).
4. Bello SM, Millo H, Rajebhosale M, Price SR (January 2012). "Catenin-dependent cadherin
function drives divisional segregation of spinal motor neurons" (https://www.ncbi.nlm.nih.gov/p
mc/articles/PMC3292792). The Journal of Neuroscience. 32 (2): 490–505.
doi:10.1523/jneurosci.4382-11.2012 (https://doi.org/10.1523%2Fjneurosci.4382-11.2012).
PMC 3292792 (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3292792). PMID 22238085 (http
s://pubmed.ncbi.nlm.nih.gov/22238085).
5. Duguay D, Foty RA, Steinberg MS (January 2003). "Cadherin-mediated cell adhesion and
tissue segregation: qualitative and quantitative determinants". Developmental Biology. 253 (2):
309–23. doi:10.1016/S0012-1606(02)00016-7 (https://doi.org/10.1016%2FS0012-1606%280
2%2900016-7). PMID 12645933 (https://pubmed.ncbi.nlm.nih.gov/12645933).
6. Niessen CM, Gumbiner BM (January 2002). "Cadherin-mediated cell sorting not determined by
binding or adhesion specificity" (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2199232). The
Journal of Cell Biology. 156 (2): 389–399. doi:10.1083/jcb.200108040 (https://doi.org/10.108
3%2Fjcb.200108040). PMC 2199232
(https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2199232). PMID 11790800 (https://pubmed.ncb
i.nlm.nih.gov/11790800).
7. Volk T, Cohen O, Geiger B (September 1987). "Formation of heterotypic adherens-type
junctions between L-CAM-containing liver cells and A-CAM-containing lens cells". Cell. 50 (6):
987–94. doi:10.1016/0092-8674(87)90525-3 (https://doi.org/10.1016%2F0092-8674%2887%2
990525-3). PMID 3621349 (https://pubmed.ncbi.nlm.nih.gov/3621349).
8. Bayas MV, Leung A, Evans E, Leckband D (February 2006). "Lifetime measurements reveal
kinetic differences between homophilic cadherin bonds" (https://www.ncbi.nlm.nih.gov/pmc/arti
cles/PMC1367289). Biophysical Journal. 90 (4): 1385–95. Bibcode:2006BpJ....90.1385B (http
s://ui.adsabs.harvard.edu/abs/2006BpJ....90.1385B). doi:10.1529/biophysj.105.069583 (https://
doi.org/10.1529%2Fbiophysj.105.069583). PMC 1367289 (https://www.ncbi.nlm.nih.gov/pmc/ar
ticles/PMC1367289). PMID 16326909 (https://pubmed.ncbi.nlm.nih.gov/16326909).
9. Harris TJ, Tepass U (July 2010). "Adherens junctions: from molecules to morphogenesis".
Nature Reviews. Molecular Cell Biology. 11 (7): 502–14. doi:10.1038/nrm2927 (https://doi.org/1
0.1038%2Fnrm2927). PMID 20571587 (https://pubmed.ncbi.nlm.nih.gov/20571587).
10. Marie PJ, Haÿ E, Modrowski D, Revollo L, Mbalaviele G, Civitelli R (January 2014). "Cadherin-
mediated cell-cell adhesion and signaling in the skeleton" (https://www.ncbi.nlm.nih.gov/pmc/ar
ticles/PMC4272239). Calcified Tissue International. 94 (1): 46–54. doi:10.1007/s00223-013-
9733-7 (https://doi.org/10.1007%2Fs00223-013-9733-7). PMC 4272239 (https://www.ncbi.nlm.
nih.gov/pmc/articles/PMC4272239). PMID 23657489 (https://pubmed.ncbi.nlm.nih.gov/236574
89).
11. Priest AV, Shafraz O, Sivasankar S (September 2017). "Biophysical basis of cadherin mediated
cell-cell adhesion". Experimental Cell Research. 358 (1): 10–13.
doi:10.1016/j.yexcr.2017.03.015 (https://doi.org/10.1016%2Fj.yexcr.2017.03.015).
PMID 28300566 (https://pubmed.ncbi.nlm.nih.gov/28300566).
12. Tepass U, Truong K, Godt D, Ikura M, Peifer M (November 2000). "Cadherins in embryonic and
neural morphogenesis". Nature Reviews. Molecular Cell Biology. 1 (2): 91–100.
doi:10.1038/35040042 (https://doi.org/10.1038%2F35040042). PMID 11253370 (https://pubme
d.ncbi.nlm.nih.gov/11253370).
13. Gumbiner BM (August 2005). "Regulation of cadherin-mediated adhesion in morphogenesis".
Nature Reviews. Molecular Cell Biology. 6 (8): 622–34. doi:10.1038/nrm1699 (https://doi.org/1
0.1038%2Fnrm1699). PMID 16025097 (https://pubmed.ncbi.nlm.nih.gov/16025097).
14. Taneyhill LA, Schiffmacher AT (June 2017). "Should I stay or should I go? Cadherin function
and regulation in the neural crest" (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5468476).
Genesis. 55 (6): n/a. doi:10.1002/dvg.23028 (https://doi.org/10.1002%2Fdvg.23028).
PMC 5468476 (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5468476). PMID 28253541 (http
s://pubmed.ncbi.nlm.nih.gov/28253541).
15. Reinhold WC, Reimers MA, Maunakea AK, Kim S, Lababidi S, Scherf U, et al. (February 2007).
"Detailed DNA methylation profiles of the E-cadherin promoter in the NCI-60 cancer cells" (http
s://doi.org/10.1158/1535-7163.MCT-06-0609). Molecular Cancer Therapeutics. 6 (2): 391–403.
doi:10.1158/1535-7163.MCT-06-0609 (https://doi.org/10.1158%2F1535-7163.MCT-06-0609).
PMID 17272646 (https://pubmed.ncbi.nlm.nih.gov/17272646).
16. Beavon IR (August 2000). "The E-cadherin-catenin complex in tumour metastasis: structure,
function and regulation". European Journal of Cancer. 36 (13 Spec No): 1607–20.
doi:10.1016/S0959-8049(00)00158-1 (https://doi.org/10.1016%2FS0959-8049%2800%290015
8-1). PMID 10959047 (https://pubmed.ncbi.nlm.nih.gov/10959047).
17. Nives Pećina-Šlaus (2003). "Tumor suppressor gene E-cadherin and its role in normal and
malignant cells" (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC270068). Cancer Cell Int. 3
(17). doi:10.1186/1475-2867-3-17 (https://doi.org/10.1186%2F1475-2867-3-17). PMC 270068
(https://www.ncbi.nlm.nih.gov/pmc/articles/PMC270068). PMID 14613514 (https://pubmed.ncbi.
nlm.nih.gov/14613514).
18. Morales CP, Souza RF, Spechler SJ (November 2002). "Hallmarks of cancer progression in
Barrett's oesophagus". Lancet. 360 (9345): 1587–9. doi:10.1016/S0140-6736(02)11569-8 (http
s://doi.org/10.1016%2FS0140-6736%2802%2911569-8). PMID 12443613 (https://pubmed.ncb
i.nlm.nih.gov/12443613).
19. Cavallaro U, Schaffhauser B, Christofori G (February 2002). "Cadherins and the tumour
progression: is it all in a switch?". Cancer Letters. 176 (2): 123–8. doi:10.1016/S0304-
3835(01)00759-5 (https://doi.org/10.1016%2FS0304-3835%2801%2900759-5).
PMID 11804738 (https://pubmed.ncbi.nlm.nih.gov/11804738).
20. Grigorian IY, Linkova NS, Polyakova VO, Paltseva EM, Kozlov KL (January 2016). "Signaling
molecules of the endometrium: Gerontological and general pathological aspects". Advances in
Gerontology. 6 (1): 36–43. doi:10.1134/S2079057016010045 (https://doi.org/10.1134%2FS207
9057016010045).
21. Harrison OJ, Jin X, Hong S, Bahna F, Ahlsen G, Brasch J, et al. (February 2011). "The
extracellular architecture of adherens junctions revealed by crystal structures of type I
cadherins" (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3070544). Structure. 19 (2): 244–56.
doi:10.1016/j.str.2010.11.016 (https://doi.org/10.1016%2Fj.str.2010.11.016). PMC 3070544 (htt
ps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3070544). PMID 21300292 (https://pubmed.ncbi.nl
m.nih.gov/21300292).
22. Stefan Offermanns; Walter Rosenthal (2008). Encyclopedia of Molecular Pharmacology (https://
books.google.com/books?id=fGe6NDIGQpsC&pg=PA306). Springer. pp. 306–. ISBN 978-3-
540-38916-3. Retrieved 14 December 2010.
23. Lodish, Harvey; Berk, Arnold; Kaiser, Chris; Krieger, Monte; Bretscher, Anthony; Ploegh, Hidde;
Amon, Angelika (2013). Molecular Cell Biology (Seventh ed.). New York: Worth Publ. p. 934.
ISBN 978-1-4292-3413-9.

Further reading
Beavon IR (August 2000). "The E-cadherin-catenin complex in tumour metastasis: structure,
function and regulation". European Journal of Cancer. 36 (13 Spec No): 1607–20.
doi:10.1016/S0959-8049(00)00158-1 (https://doi.org/10.1016%2FS0959-8049%2800%290015
8-1). PMID 10959047 (https://pubmed.ncbi.nlm.nih.gov/10959047).
Berx G, Becker KF, Höfler H, van Roy F (1998). "Mutations of the human E-cadherin (CDH1)
gene". Human Mutation. 12 (4): 226–37. doi:10.1002/(SICI)1098-1004(1998)12:4<226::AID-
HUMU2>3.0.CO;2-D (https://doi.org/10.1002%2F%28SICI%291098-1004%281998%2912%3A
4%3C226%3A%3AAID-HUMU2%3E3.0.CO%3B2-D). PMID 9744472 (https://pubmed.ncbi.nl
m.nih.gov/9744472).
Bryant DM, Stow JL (August 2004). "The ins and outs of E-cadherin trafficking". Trends in Cell
Biology. 14 (8): 427–34. doi:10.1016/j.tcb.2004.07.007 (https://doi.org/10.1016%2Fj.tcb.2004.0
7.007). PMID 15308209 (https://pubmed.ncbi.nlm.nih.gov/15308209).
Chun YS, Lindor NM, Smyrk TC, Petersen BT, Burgart LJ, Guilford PJ, Donohue JH (July
2001). "Germline E-cadherin gene mutations: is prophylactic total gastrectomy indicated?".
Cancer. 92 (1): 181–7. doi:10.1002/1097-0142(20010701)92:1<181::AID-
CNCR1307>3.0.CO;2-J (https://doi.org/10.1002%2F1097-0142%2820010701%2992%3A1%3
C181%3A%3AAID-CNCR1307%3E3.0.CO%3B2-J). PMID 11443625 (https://pubmed.ncbi.nl
m.nih.gov/11443625).
Georgolios A, Batistatou A, Manolopoulos L, Charalabopoulos K (March 2006). "Role and
expression patterns of E-cadherin in head and neck squamous cell carcinoma (HNSCC)".
Journal of Experimental & Clinical Cancer Research. 25 (1): 5–14. PMID 16761612 (https://pub
med.ncbi.nlm.nih.gov/16761612).
Hazan RB, Qiao R, Keren R, Badano I, Suyama K (April 2004). "Cadherin switch in tumor
progression". Annals of the New York Academy of Sciences. 1014 (1): 155–63.
Bibcode:2004NYASA1014..155H (https://ui.adsabs.harvard.edu/abs/2004NYASA1014..155H).
doi:10.1196/annals.1294.016 (https://doi.org/10.1196%2Fannals.1294.016). PMID 15153430
(https://pubmed.ncbi.nlm.nih.gov/15153430).
Moran CJ, Joyce M, McAnena OJ (April 2005). "CDH1 associated gastric cancer: a report of a
family and review of the literature". European Journal of Surgical Oncology. 31 (3): 259–64.
doi:10.1016/j.ejso.2004.12.010 (https://doi.org/10.1016%2Fj.ejso.2004.12.010).
PMID 15780560 (https://pubmed.ncbi.nlm.nih.gov/15780560).
Reynolds AB, Carnahan RH (December 2004). "Regulation of cadherin stability and turnover
by p120ctn: implications in disease and cancer". Seminars in Cell & Developmental Biology.
15 (6): 657–63. doi:10.1016/j.semcdb.2004.09.003 (https://doi.org/10.1016%2Fj.semcdb.2004.
09.003). PMID 15561585 (https://pubmed.ncbi.nlm.nih.gov/15561585).
Wang HD, Ren J, Zhang L (November 2004). "CDH1 germline mutation in hereditary gastric
carcinoma" (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4611247). World Journal of
Gastroenterology. 10 (21): 3088–93. doi:10.3748/wjg.v10.i21.3088 (https://doi.org/10.3748%2F
wjg.v10.i21.3088). PMC 4611247 (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4611247).
PMID 15457549 (https://pubmed.ncbi.nlm.nih.gov/15457549).
Wijnhoven BP, Dinjens WN, Pignatelli M (August 2000). "E-cadherin-catenin cell-cell adhesion
complex and human cancer" (http://repub.eur.nl/pub/56571). The British Journal of Surgery. 87
(8): 992–1005. doi:10.1046/j.1365-2168.2000.01513.x (https://doi.org/10.1046%2Fj.1365-2168.
2000.01513.x). hdl:1765/56571 (https://hdl.handle.net/1765%2F56571). PMID 10931041 (http
s://pubmed.ncbi.nlm.nih.gov/10931041).
Wilson PD (April 2001). "Polycystin: new aspects of structure, function, and regulation". Journal
of the American Society of Nephrology. 12 (4): 834–45. PMID 11274246 (https://pubmed.ncbi.nl
m.nih.gov/11274246).
Renaud-Young M, Gallin WJ (October 2002). "In the first extracellular domain of E-cadherin,
heterophilic interactions, but not the conserved His-Ala-Val motif, are required for adhesion" (htt
ps://doi.org/10.1074/jbc.M201256200). The Journal of Biological Chemistry. 277 (42): 39609–
16. doi:10.1074/jbc.M201256200 (https://doi.org/10.1074%2Fjbc.M201256200).
PMID 12154084 (https://pubmed.ncbi.nlm.nih.gov/12154084).
External links
Proteopedia Cadherin (http://www.proteopedia.org/wiki/index.php/Cadherin) - view cadherin
structure in interactive 3D
Cadherin domain (http://prosite.expasy.org/PDOC00205) in PROSITE
The cadherin family (https://web.archive.org/web/20060925073601/http://www.gene.ucl.ac.uk/n
omenclature/genefamily/cdh.php)
Alberts, Bruce. Molecular Biology of the Cell (https://www.ncbi.nlm.nih.gov/sites/entrez?db=boo
ks&doptcmdl=DocSum&term=cadherin+AND+mboc4%5Bbook%5D)
The Cadherin Resource (http://calcium.uhnres.utoronto.ca/cadherin/pub_pages/general/intro_c
adherins.htm)
InterPro: IPR002126 (https://www.ebi.ac.uk/interpro/entry/IPR002126)
[1] (http://www.copewithcytokines.org/cope.cgi?key=N-cadherin)
"Cadherin (http://jcs.biologists.org/content/126/2/373)adhesome at a glance". J Cell Sci 126,
373-378

Retrieved from "https://en.wikipedia.org/w/index.php?title=Cadherin&oldid=972025048"

This page was last edited on 9 August 2020, at 19:05 (UTC).

Text is available under the Creative Commons Attribution-ShareAlike License; additional terms may apply. By using this
site, you agree to the Terms of Use and Privacy Policy. Wikipedia® is a registered trademark of the Wikimedia
Foundation, Inc., a non-profit organization.