Cell No. : Cell Name RCB1699 : LY-B/cLCB1  update : 2023/09/21
Comment			LY-B derivative complemented the Serine-palmitoyl transferase (LCB1 subunit) deficiency.
Comment from the depositor
Terms and conditions			In publishing research results obtained by the use of the BIOLOGICAL RESOURCE, a citation of the literature ref. (J Biol Chem 1998;273:33787-33794) designated by the DEPOSITOR is required.
Remarks
Order Form			Order Form(C-0005.pdf)   MTA(C-0007.pdf)   MTA(C-0007p.pdf)
			Regarding MTA between user institutions and RIKEN BRC, there are two kinds of MTA, not-for-profit academic purpose (C-XXXX) and for-profit research purpose (C-XXXXp) , depending on the sort of user institutions and the purposes of use. Please use an appropriate MTA(to see). In relation to commercial use and use for patent filing, first of all Please contact RIKEN BRC (cellbank.brc@riken.jp).
	Basic information	Depositor	Hanada, Kentaro
		Originator	Hanada, Kentaro
		Year of deposit	2000
		Original cell	CHO-K1
		Animal	_hamster < Mammals
		Strain name	Chinese
		Genus	Cricetulus
		Species	griseus
		Gender	Female
		Age at sampling	adult
		Tissue	ovary
		Classification	mutant
		Recombinant	recombinant
		Exogene	pSV-OKneo, LCB1 gene cDNA
		Lifespan	infinite
		Morphology	fibroblast-like
		Cellosaurus(Expasy)	CVCL_U862
			deposit info	lot info
		Medium	Medium List
		Culture type		Adherent cells
		Culture medium		HamF12 + 10% NBS (or FBS)
		Antibiotics		Free
		Passage method		0.25% Trypsin
	Culture information	Passage cell No		1-5 x 10 5 cell/100 mm dish
		Passage ratio		1 : 8 split
		SC frequency		Subculture : 2 times/week
		Temperature		33 ℃
		CO2 concentration		5 %
		Freeze medium		Medium + 10% DMSO
		Freezing method		Slow freezing
		Mycoplasma/Acholeplasma		(-)
		Animal PCR		OK
		Isozyme		LD, NP, MPI, PepB
Reference information		Reference	2
		User's Publication	2

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Reference

2687  Hanada K, Hara T, Fukasawa M, Yamaji A, Umeda M, Nishijima M  Mammalian cell mutants resistant to a sphingomyelin-directed cytolysin. Genetic and biochemical evidence for complex formation of the LCB1 protein with the LCB2 protein for serine palmitoyltransferase.  J Biol Chem  1998  273:33787-94  PubMed ID: 9837968   DOI: 10.1074/jbc.273.50.33787

2686  Hanada K, Hara T, Nishijima M, Kuge O, Dickson, R C, Nagiec, M M  A mammalian homolog of the yeast LCB1 encodes a component of serine palmitoyltransferase, the enzyme catalyzing the first step in sphingolipid synthesis.  J Biol Chem  1997  272:32108-14  PubMed ID: 9405408   DOI: 10.1074/jbc.272.51.32108

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User's Publication

22093  Linton C, Wesolowski J, Lobley A, Yamaji T, Hanada K, Paumet F.  Specialized contact sites regulate the fusion of chlamydial inclusion membranes.  Nat Commun  2024  15(1):9250  PubMed ID: 39461996   DOI: 10.1038/s41467-024-53443-7

8301  Eshraghi A, Maldonado-Arocho FJ, Gargi A, Cardwell MM, Prouty MG, Blanke SR, Bradley KA.  Cytolethal distending toxin family members are differentially affected by alterations in host glycans and membrane cholesterol.  J. Biol. Chem.  2010  285:18199-207  PubMed ID: 20385557   DOI: 10.1074/jbc.M110.112912