Nidogen
Nidogens, formerly known as entactins, are a family of sulfated monomeric glycoproteins located in the basal lamina[1] of parahoxozoans.[2] Two nidogens have been identified in humans: nidogen-1 (NID1) and nidogen-2 (NID2).[3] Remarkably, vertebrates are still capable of stabilizing basement membrane in the absence of either identified nidogen.[4] In contrast, those lacking both nidogen-1 and nidogen-2 typically die prematurely during embryonic development as a result of defects existing in the heart and lungs.[5] Nidogen have been shown to play a crucial role during organogenesis in late embryonic development, particularly in cardiac and lung development.[6] Insufficient levels of nidogen in mice causes poorly developed organs such as the lungs and heart, which ultimately ensues to an early death.[7] Due to nidogen being necessary in the formation of basement membranes, serving as a linker protein, and those basement proteins being shown to be necessary during tissue growth, nidogen is crucial for embryonic development.[8] From an evolutionary perspective, nidogens are highly conserved across vertebrates and invertebrates, retaining their ability to bind laminin.[9]
In nematodes, nidogen-1 is necessary for axon guidance, but not for basement membrane assembly.[10]
References[edit]
- ^ Hortsch M, Umemori H (2009). The Sticky Synapse: Cell Adhesion Molecules and Their Role in Synapse Formation and Maintenance. New York, NY: Springer. p. 66. ISBN 9780387927084.
- ^ Nielsen C (July 2019). "Early animal evolution: a morphologist's view". Royal Society Open Science. 6 (7): 190638. Bibcode:2019RSOS....690638N. doi:10.1098/rsos.190638. PMC 6689584. PMID 31417759.
- ^ Miosge N, Holzhausen S, Zelent C, Sprysch P, Herken R (2001). "Nidogen-1 and nidogen-2 are found in basement membranes during human embryonic development". The Histochemical Journal. 33 (9–10): 523–530. doi:10.1023/A:1014995523521. PMID 12005023. S2CID 818451.
- ^ Lössl P, Kölbel K, Tänzler D, Nannemann D, Ihling CH, Keller MV, et al. (2014-11-11). Kobe B (ed.). "Analysis of nidogen-1/laminin γ1 interaction by cross-linking, mass spectrometry, and computational modeling reveals multiple binding modes". PLOS ONE. 9 (11): e112886. Bibcode:2014PLoSO...9k2886L. doi:10.1371/journal.pone.0112886. PMC 4227867. PMID 25387007.
- ^ Fox MA, Ho MS, Smyth N, Sanes JR (September 2008). "A synaptic nidogen: developmental regulation and role of nidogen-2 at the neuromuscular junction". Neural Development. 3 (1): 24. doi:10.1186/1749-8104-3-24. PMC 2567315. PMID 18817539.
- ^ Bader BL, Smyth N, Nedbal S, Miosge N, Baranowsky A, Mokkapati S, et al. (August 2005). "Compound genetic ablation of nidogen 1 and 2 causes basement membrane defects and perinatal lethality in mice". Molecular and Cellular Biology. 25 (15): 6846–6856. doi:10.1128/MCB.25.15.6846-6856.2005. PMC 1190363. PMID 16024816.
- ^ Lakshmanan HH, Melrose AR, Sepp AI, Mitrugno A, Ngo AT, Khader A, et al. (April 2021). "The basement membrane protein nidogen-1 supports platelet adhesion and activation". Platelets. 32 (3): 424–428. doi:10.1080/09537104.2020.1745170. PMC 8559984. PMID 32233694.
- ^ Dziadek M (September 1995). "Role of laminin-nidogen complexes in basement membrane formation during embryonic development". Experientia. 51 (9–10): 901–913. doi:10.1007/BF01921740. PMID 7556571.
- ^ Mayer U, Kohfeldt E, Timpl R (October 1998). "Structural and genetic analysis of laminin-nidogen interaction". Annals of the New York Academy of Sciences. 857 (1): 130–142. Bibcode:1998NYASA.857..130M. doi:10.1111/j.1749-6632.1998.tb10113.x. PMID 9917838. S2CID 36725654.
- ^ Kim S, Wadsworth WG (April 2000). "Positioning of longitudinal nerves in C. elegans by nidogen". Science. 288 (5463): 150–154. Bibcode:2000Sci...288..150K. doi:10.1126/science.288.5463.150. PMID 10753123.
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