RBCC

BPI [Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Bactericidal permeability-increasing protein; BPI (CAP 57; Flags: Precursor)

UniProt P17213
ID BPI_HUMAN Reviewed; 487 AA.
AC P17213; B2RCY2; Q1ZZU8; Q5JRW0; Q8IW58; Q9BYZ9; Q9H1L2; Q9H1M8;
read moreAC Q9H203; Q9UCT4; Q9UD65;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 4.
DT 22-JAN-2014, entry version 141.
DE RecName: Full=Bactericidal permeability-increasing protein;
DE Short=BPI;
DE AltName: Full=CAP 57;
DE Flags: Precursor;
GN Name=BPI;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 32-68, FUNCTION,
RP SUBCELLULAR LOCATION, DOMAIN, AND VARIANTS VAL-16 AND LYS-216.
RX PubMed=2722846;
RA Gray P.W., Flaggs G., Leong S.R., Gumina R.J., Weiss J., Ooi C.E.,
RA Elsbach P.;
RT "Cloning of the cDNA of a human neutrophil bactericidal protein.
RT Structural and functional correlations.";
RL J. Biol. Chem. 264:9505-9509(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7517398;
RA Wilde C.G., Seilhamer J.J., McGrogan M., Ashton N., Snable J.L.,
RA Lane J.C., Leong S.R., Thornton M.B., Miller K.L., Scott R.W.;
RT "Bactericidal/permeability-increasing protein and lipopolysaccharide
RT (LPS)-binding protein. LPS binding properties and effects on LPS-
RT mediated cell activation.";
RL J. Biol. Chem. 269:17411-17416(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-16.
RA Ma H., Cao X., Sun Y., Lei W.;
RT "cDNA cloning and sequence analysis of human bactericidal/permeability
RT protein.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-404.
RC TISSUE=Fetal heart;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-216.
RC TISSUE=Leukocyte;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-487, AND VARIANTS LYS-216 AND ASP-404.
RA Xu J., Wang H.;
RT "Cloning of cDNA of human bactericidal/permeability-increasing
RT protein.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP PROTEIN SEQUENCE OF 32-53, AND FUNCTION.
RC TISSUE=Leukocyte;
RX PubMed=1937776;
RA Wasiluk K.R., Skubitz K.M., Gray B.H.;
RT "Comparison of granule proteins from human polymorphonuclear
RT leukocytes which are bactericidal toward Pseudomonas aeruginosa.";
RL Infect. Immun. 59:4193-4200(1991).
RN [9]
RP PROTEIN SEQUENCE OF 32-51.
RX PubMed=2501794; DOI=10.1073/pnas.86.14.5610;
RA Gabay J.E., Scott R.W., Campanelli D., Griffith J., Wilde C.,
RA Marra M.N., Seeger M., Nathan C.F.;
RT "Antibiotic proteins of human polymorphonuclear leukocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:5610-5614(1989).
RN [10]
RP PROTEIN SEQUENCE OF 32-48.
RX PubMed=3667613;
RA Ooi C.E., Weiss J., Elsbach P., Frangione B., Mannion B.;
RT "A 25-kDa NH2-terminal fragment carries all the antibacterial
RT activities of the human neutrophil 60-kDa bactericidal/permeability-
RT increasing protein.";
RL J. Biol. Chem. 262:14891-14894(1987).
RN [11]
RP SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-49; CYS-163;
RP CYS-166 AND CYS-206.
RX PubMed=8812832; DOI=10.1006/prep.1996.0071;
RA Horwitz A.H., Leigh S.D., Abrahamson S., Gazzano-Santoro H.,
RA Liu P.-S., Williams R.E., Carroll S.F., Theofan G.;
RT "Expression and characterization of cysteine-modified variants of an
RT amino-terminal fragment of bactericidal/permeability-increasing
RT protein.";
RL Protein Expr. Purif. 8:28-40(1996).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 32-487.
RX PubMed=9188532; DOI=10.1126/science.276.5320.1861;
RA Beamer L.J., Carroll S.F., Eisenberg D.;
RT "Crystal structure of human BPI and two bound phospholipids at 2.4-A
RT resolution.";
RL Science 276:1861-1864(1997).
CC -!- FUNCTION: The cytotoxic action of BPI is limited to many species
CC of Gram-negative bacteria; this specificity may be explained by a
CC strong affinity of the very basic N-terminal half for the
CC negatively charged lipopolysaccharides that are unique to the
CC Gram-negative bacterial outer envelope. Has antibacterial activity
CC against the Gram-nagative bacterium P.aeruginosa, this activity is
CC inhibited by LPS from P.aeruginosa.
CC -!- SUBUNIT: Monomer. Homodimer; disulfide-linked.
CC -!- SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule membrane.
CC Note=Membrane-associated in polymorphonuclear Leukocytes (PMN)
CC granules.
CC -!- TISSUE SPECIFICITY: Restricted to cells of the myeloid series.
CC -!- DOMAIN: The N-terminal region may be exposed to the interior of
CC the granule, whereas the C-terminal portion may be embedded in the
CC membrane. During phagocytosis and degranulation, proteases may be
CC released and activated and cleave BPI at the junction of the N-
CC and C-terminal portions of the molecule, providing controlled
CC release of the N-terminal antibacterial fragment when bacteria are
CC ingested.
CC -!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP
CC family.
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DR EMBL; J04739; AAA51841.1; -; mRNA.
DR EMBL; DQ414688; ABD66755.1; -; mRNA.
DR EMBL; AK315328; BAG37729.1; -; mRNA.
DR EMBL; AL359555; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL391095; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL499625; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL583962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC040955; AAH40955.1; -; mRNA.
DR EMBL; AF322588; AAG42844.1; -; mRNA.
DR PIR; A33850; A30909.
DR RefSeq; NP_001716.2; NM_001725.2.
DR UniGene; Hs.529019; -.
DR PDB; 1BP1; X-ray; 2.40 A; A=32-487.
DR PDB; 1EWF; X-ray; 1.70 A; A=32-483.
DR PDBsum; 1BP1; -.
DR PDBsum; 1EWF; -.
DR ProteinModelPortal; P17213; -.
DR SMR; P17213; 32-487.
DR TCDB; 1.C.40.1.1; the bactericidal permeability increasing protein (bpip) family.
DR PhosphoSite; P17213; -.
DR DMDM; 215274242; -.
DR PaxDb; P17213; -.
DR PRIDE; P17213; -.
DR Ensembl; ENST00000262865; ENSP00000262865; ENSG00000101425.
DR GeneID; 671; -.
DR KEGG; hsa:671; -.
DR UCSC; uc002xib.2; human.
DR CTD; 671; -.
DR GeneCards; GC20P036888; -.
DR H-InvDB; HIX0027669; -.
DR HGNC; HGNC:1095; BPI.
DR MIM; 109195; gene.
DR neXtProt; NX_P17213; -.
DR PharmGKB; PA25403; -.
DR eggNOG; NOG262970; -.
DR HOVERGEN; HBG002797; -.
DR InParanoid; P17213; -.
DR OMA; CSSHINS; -.
DR PhylomeDB; P17213; -.
DR ChiTaRS; BPI; human.
DR EvolutionaryTrace; P17213; -.
DR GenomeRNAi; 671; -.
DR NextBio; 2748; -.
DR PRO; PR:P17213; -.
DR ArrayExpress; P17213; -.
DR Bgee; P17213; -.
DR Genevestigator; P17213; -.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
DR GO; GO:0001530; F:lipopolysaccharide binding; IDA:BHF-UCL.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0006955; P:immune response; IEA:Ensembl.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; IDA:BHF-UCL.
DR GO; GO:0032717; P:negative regulation of interleukin-8 production; IDA:BHF-UCL.
DR GO; GO:0043031; P:negative regulation of macrophage activation; IDA:BHF-UCL.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IDA:BHF-UCL.
DR InterPro; IPR017943; Bactericidal_perm-incr_a/b_dom.
DR InterPro; IPR001124; Lipid-bd_serum_glycop_C.
DR InterPro; IPR017954; Lipid-bd_serum_glycop_CS.
DR InterPro; IPR017942; Lipid-bd_serum_glycop_N.
DR Pfam; PF01273; LBP_BPI_CETP; 1.
DR Pfam; PF02886; LBP_BPI_CETP_C; 1.
DR SMART; SM00328; BPI1; 1.
DR SMART; SM00329; BPI2; 1.
DR SUPFAM; SSF55394; SSF55394; 2.
DR PROSITE; PS00400; LBP_BPI_CETP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Complete proteome;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Membrane;
KW Polymorphism; Reference proteome; Secreted; Signal.
FT SIGNAL 1 31
FT CHAIN 32 487 Bactericidal permeability-increasing
FT protein.
FT /FTId=PRO_0000017154.
FT REGION 240 245 Cleavage sites for elastase (Potential).
FT CARBOHYD 380 380 N-linked (GlcNAc...) (Potential).
FT DISULFID 166 206
FT VARIANT 12 12 A -> T (in dbSNP:rs5743497).
FT /FTId=VAR_049728.
FT VARIANT 12 12 A -> V (in dbSNP:rs5743498).
FT /FTId=VAR_049729.
FT VARIANT 16 16 A -> V (in dbSNP:rs1341023).
FT /FTId=VAR_018401.
FT VARIANT 90 90 R -> C (in dbSNP:rs5743500).
FT /FTId=VAR_049730.
FT VARIANT 140 140 E -> Q (in dbSNP:rs5743506).
FT /FTId=VAR_049732.
FT VARIANT 196 196 A -> V (in dbSNP:rs5743509).
FT /FTId=VAR_018402.
FT VARIANT 216 216 E -> K (in dbSNP:rs4358188).
FT /FTId=VAR_018403.
FT VARIANT 280 280 A -> V (in dbSNP:rs5741804).
FT /FTId=VAR_049733.
FT VARIANT 377 377 V -> I (in dbSNP:rs5743524).
FT /FTId=VAR_049734.
FT VARIANT 404 404 N -> D (in dbSNP:rs5741809).
FT /FTId=VAR_049735.
FT VARIANT 451 451 K -> E (in dbSNP:rs5743542).
FT /FTId=VAR_049736.
FT MUTAGEN 49 49 S->C: No impairment of secretion and
FT increased propensity for dimer formation.
FT MUTAGEN 163 163 C->A: No impairment of secretion and/or
FT biological activity. Loss of dimer
FT formation.
FT MUTAGEN 166 166 C->S: Poorly secreted. Loss of LPS-
FT binding and biological activity.
FT MUTAGEN 206 206 C->A: Not secreted.
FT CONFLICT 5 5 M -> L (in Ref. 6; AAH40955).
FT CONFLICT 53 53 T -> R (in Ref. 8; AA sequence).
FT CONFLICT 355 355 P -> S (in Ref. 7; AAG42844).
FT CONFLICT 375 375 F -> L (in Ref. 2).
FT CONFLICT 411 411 K -> R (in Ref. 7; AAG42844).
FT CONFLICT 433 433 Q -> L (in Ref. 4; BAG37729).
FT STRAND 35 41
FT HELIX 42 60
FT STRAND 68 71
FT STRAND 75 79
FT STRAND 81 93
FT STRAND 97 102
FT TURN 103 105
FT STRAND 106 126
FT STRAND 129 153
FT TURN 154 157
FT STRAND 158 169
FT STRAND 172 176
FT HELIX 180 182
FT HELIX 183 192
FT HELIX 194 215
FT HELIX 217 221
FT STRAND 226 229
FT STRAND 231 233
FT STRAND 235 237
FT STRAND 240 242
FT STRAND 248 255
FT STRAND 258 260
FT STRAND 282 290
FT HELIX 291 303
FT STRAND 307 312
FT HELIX 313 315
FT HELIX 326 330
FT STRAND 333 335
FT HELIX 336 339
FT STRAND 344 350
FT STRAND 356 360
FT STRAND 363 367
FT STRAND 369 377
FT STRAND 383 392
FT STRAND 395 401
FT STRAND 403 412
FT STRAND 416 424
FT HELIX 429 432
FT HELIX 433 443
FT HELIX 445 454
FT STRAND 464 474
FT STRAND 477 486
SQ SEQUENCE 487 AA; 53900 MW; 30BC73B1B465B62D CRC64;
MRENMARGPC NAPRWASLMV LVAIGTAVTA AVNPGVVVRI SQKGLDYASQ QGTAALQKEL
KRIKIPDYSD SFKIKHLGKG HYSFYSMDIR EFQLPSSQIS MVPNVGLKFS ISNANIKISG
KWKAQKRFLK MSGNFDLSIE GMSISADLKL GSNPTSGKPT ITCSSCSSHI NSVHVHISKS
KVGWLIQLFH KKIESALRNK MNSQVCEKVT NSVSSELQPY FQTLPVMTKI DSVAGINYGL
VAPPATTAET LDVQMKGEFY SENHHNPPPF APPVMEFPAA HDRMVYLGLS DYFFNTAGLV
YQEAGVLKMT LRDDMIPKES KFRLTTKFFG TFLPEVAKKF PNMKIQIHVS ASTPPHLSVQ
PTGLTFYPAV DVQAFAVLPN SSLASLFLIG MHTTGSMEVS AESNRLVGEL KLDRLLLELK
HSNIGPFPVE LLQDIMNYIV PILVLPRVNE KLQKGFPLPT PARVQLYNVV LQPHQNFLLF
GADVVYK
//

MIM 109195
*RECORD*
*FIELD* NO
109195
*FIELD* TI
*109195 BACTERICIDAL PERMEABILITY-INCREASING PROTEIN; BPI
*FIELD* TX

DESCRIPTION

read moreThe bactericidal permeability-increasing protein (BPI) is associated
with human neutrophil granules and has bactericidal activity on
gram-negative organisms. Both BPI and lipopolysaccharide-binding protein
(LBP; 151990) are involved in the defense against gram-negative
bacterial infections and bind LPS with high affinity. Furthermore, they
show 44% amino acid identity (Schumann et al., 1990).

CLONING

Using oligonucleotides derived from the human BPI protein sequence to
screen a human genomic library, Gray et al. (1989) isolated BPI genomic
sequence. They screened a dimethyl sulfoxide-induced HL-60 cell cDNA
library with oligonucleotides based on the genomic sequence and isolated
a full-length human BPI cDNA. The cDNA predicts a 31-amino acid signal
peptide followed by a 456-amino acid mature protein. The N-terminal half
of the protein, which exhibits the antimicrobial activity, is basic and
hydrophilic, whereas the C-terminal half is slightly acidic and contains
several potential transmembrane regions. The difference between the
calculated molecular mass of 50.6 kD and the experimental mass of
approximately 58 kD may reflect the usage of 2 potential N-linked
glycosylation sites. Northern blot analysis detected a 2-kb BPI
transcript in mRNA prepared from the spleen of a patient with chronic
myelogenous leukemia (CML; 608232); a lower level of BPI expression was
found in normal spleen, but no BPI expression was detected in normal
liver, placenta, or brain.

GENE STRUCTURE

Hubacek et al. (1997) found that the BPI gene spans approximately 31.5
kb of DNA and contains 15 exons. Comparison of the genomic structures of
BPI, LBP, PLTP (172425), and CETP (118470), which constitute a family of
functionally related proteins, revealed a remarkable conservation of
exon/intron junctions and exon size.

MAPPING

Using both Southern blot analysis of human/mouse somatic cell hybrids
and in situ hybridization, Gray et al. (1993) mapped the BPI and LBP
genes to 20q11.23-q12.

*FIELD* RF
1. Gray, P. W.; Corcorran, A. E.; Eddy, R. L., Jr.; Byers, M. G.;
Shows, T. B.: The genes for the lipopolysaccharide binding protein
(LBP) and the bactericidal permeability increasing protein (BPI) are
encoded in the same region of human chromosome 20. Genomics 15:
188-190, 1993.

2. Gray, P. W.; Flaggs, G.; Leong, S. R.; Gumina, R. J.; Weiss, J.;
Ooi, C. E.; Elsbach, P.: Cloning of the cDNA of a human neutrophil
bactericidal protein: structural and functional correlations. J.
Biol. Chem. 264: 9505-9509, 1989.

3. Hubacek, J. A.; Buchler, C.; Aslanidis, C.; Schmitz, G.: The genomic
organization of the genes for human lipopolysaccharide binding protein
(LBP) and bactericidal permeability increasing protein (BPI) is highly
conserved. Biochem. Biophys. Res. Commun. 236: 427-430, 1997.

4. Schumann, R. R.; Leong, S. R.; Flaggs, G. W.; Gray, P. W.; Wright,
S. D.; Mathison, J. C.; Tobias, P. S.; Ulevitch, R. J.: Structure
and function of lipopolysaccharide binding protein. Science 249:
1429-1431, 1990.

*FIELD* CN
Sheryl A. Jankowski - updated: 8/5/1999

*FIELD* CD
Victor A. McKusick: 2/17/1993

*FIELD* ED
alopez: 07/16/2012
alopez: 11/17/2003
psherman: 8/6/1999
psherman: 8/5/1999
carol: 2/17/1993

RBCC Red Blood Cell Collection

Full text data of BPI