214
Biochimica et Biophysica Acta, 1131 (1992) 214-216 © 1992 Elsevier Science Publishers B.V. All rights reserved 0167-4781/92/$05.00
BBAEXP 90359
Short Sequence-Paper
Nucleotide sequence of rat vascular cell adhesion molecule-1 c D N A A m y J. Williams a Robert C. Atkins b, J o c h e n W.U. Fries a Michael A. G i m b r o n e Jr. a, Myron I. Cybulsky a and Tucker Collins a " Vascular Research Division, Department of Pathology, Brigham and Women's Hospital, Harl,ard Medical School, Boston, MA (USA) and b Department of Nephrology, Monash Medical Center, Clayton (Australia) (Received 27 February 1992)
Key words: Nucleotide sequence; Adhesion molecule-i; (Rat vascular cell)
Vascular cell adhesion molecule 1 (VCAM-1) is an inducible transmembrane protein which is expressed by vascular endothelium following cytokine activation. VCAM-I mediated the adhesion of certain blood leukocytes and tumor cells via the interaction with its counter-receptor, the integrin VLA4 [1]. When initially cloned from interleukin-1 (IL-1) stimulated human umbilical vein endothelial cells, VCAM-1 was reported to contain six immunoglobulin-like domains [2]. However, subsequent cDNA clones [3-5] and structural analysis of the human gene [6] revealed an alternatively spliced seventh immunoglobulin domain. This seven domain form appears to be the predominant transcript in IL-1 activated endothelium [3,4]. In this report, the cloning and nucleotide sequence of rat VCAM-1 is described.
The complete open reading frame of rat VCAM-1 was generated by polymerase chain reaction (PCR) using nested oligonucleotide primers. Total R N A was prepared from lipopolysaccharide treated (4 h) rat lungs by a guanidine isothiocyanate protocol. Reverse transcriptase was used to synthesize first strand c D N A from 1 /.tg of the rat RNA, and three overlapping regions of VCAM-1 c D N A were amplified using three sets of nested P C R primers (four different primers per set). Primers were chosen from regions of the VCAM-1 molecule which contained the greatest degree of conservation based on nucleotide homologies between the human and the rabbit sequences (Cybulskry et al., unpublished data). Three independent clones were sequenced from each of the three nested sets of primers in order to resolve sequence discrepancies due to P C R generated errors.
Correspondence to: T. Collins, Vascular Research Division, Department of Pathology, Brigham and Women's Hospital, 221 Longwood Avenue, Boston, MA 02115, USA.
The c D N A denoted in Fig. 1 has an open reading frame of 2220 base pairs which codes for a protein of 740 amino acids and contains the alternatively spliced domain 4. Rat VCAM-1 showed more than 77% amino acid identity with the rabbit and human proteins (Fig. 2). Like the human form, rat VCAM-1 has internal homology, with domains 1 and 4 being the most homologous (62%). Conservation of this internal repeat is consistent with recent observations that both domains 1 and 4 contain functional binding sites for counter-receptor (Osborn et al., unpublished data). An independent determination of the D N A sequence of a rat VCAM-1 c D N A was recently reported [7]. Two nucleotide differences within the coding region were noted at positions 502 (G to A) and 504 (T to C), which result in a single change in amino acids from Asp to Asn. Sequence analysis of additional rat VCAM-1 cDNAs should reveal whether this is a polymorphism or a P C R generated structural alteration. Since the rat is an important species model for the study of several immune and inflammatory processes, the isolation and characterization of a rat VCAM-1 c D N A will serve as a useful tool to study VCAM-1 pathophysiology.
215 1 101 201 301 401 501 601 701 801 901 i001 1101 1201 1301 1401 1501 1601 1701 1801 1901 2 0 01 2101 2201
TTTAAAATGCCTGGGAAGATGGTCGCGATCTTCGGAG CCTCAACGGTACTTTGGATACTGTTTGCAGTCTCTCAAG CTTTTaAAATCGAGATCTCCCCTG M P G K M V A I F G A S T V L W I L F A V S Q A F K I E I S P E AATACAAAACGCTCGCTCAGATTGGAGACTCCATGCTCCTGACTTGCAGCACCACAGG CTGTGAGTCGCCATCATTCTCTTGGAGAACCCAGATAGACAG ¥ K T L A Q I G D S M L L T C S T T G C E S P S F S W R T Q I D S TCCACTAAATGGGAAGGTGAAGACAGAGGGGGCCAAGTCCGTTCTGACCATGGACCCTGTCAGCTTTGAGAATGAACACTCTTACCTGTGCACAGCAACA P L N G K V K T E G A K S V L T M D P V S F E N E H S ¥ L C T A T TGTAACTCTGGGAAACTGGAAAGAGGAATCCAAGTGGACATCTACTCATTCCCTAAGGATCCAGAGATTCAATTCAGTGGCCCCCTGGAGGTTGGGAAGC C N S G K L E R G I Q V D I Y S F P K D P E I Q F S G P L E V G K P CGGTCATGGTCAAGTGTTTGGCTCCTGATGTTTACCCAATTGACAGACTGGAGATAGAACTGTTCAAGGGTGAC•GTCTCATGAAGAAACAGGATTTTGT V M V K C L A P D V Y P I D R L E I E L F K G D R L M K K Q D F V AAACGAGATGGCAAAGAAGTCTCTGGAAACCAAGAGTTTGGAAGTCATCTTTACTCCTGTCATTGAGGATATTGAAAAGGCTCTTGTTTGCC GAGCTAAA N E M A K K S L E T K S L E V I F T P V I E D I E K A L V C R A K TTATACATTGACCAAACTGATTCTATTCCCAAAGAAAGGGAGACTGTCAGAGAACTACAAGTCTACACCTCCCCCAAGAATACAGAGATCTCTGTACATC L Y I D Q T D S I P K E R E T V R E L Q V ¥ T S P K N T E I S V H P CCTCCACAAGG CTACATGAGGGTG CTGCTGTGACGATGACATGTGCCAG CGAGGGTCTACCAGCTCCTGAGA'FFFI'CTGGAGCAAGAAATTAGATAATGG S T R L H E G A A V T M T C A S E G L P A P E I F W S K K L D N G AGTTCTACAGCTCCTCTCGGGAAATGCCACCCTCACCTTAATTGCTATGAGGATGGAAGATTCTGGAATCTATGTGTGTGAAGGAGTGAATCTGGTTGGG V L Q L L S G N A T L T L I A M R M E D S G I Y V C E G V N L V G AGAGACAAAACAGAAGTGGAATTAATTGTTCAAGAGAAACCATTTACTGTTGACATCTCCC CTGGATCTCAGGTGGCTGCACAGGTTGGGGATTCCGTTG R D K T E V E L I V Q E K P F T V D I S P G S Q V A A Q V G D S V V TTCTGACATGTGCTGCTGTTGGCTGTGACTCTCC CTCC'FFFI'CTTGGAGAACCCAGACAGACAGTCCCCTCAATGGGGAGGTGAGGGATGAAGGGG CTAC L T C A A V G C D S P S F S W R T Q T D S P L N G E V R D E G A T ATCCACACTGACG CTGAG CC CTGTGGGTGTTGAGGATGAGCACTCTTACCTGTGCACTGTGACCTGTCAG CGAAGGAAACTGGAGAAGACAATCCAAGTG S T L T L S P V G V E D E H S ¥ L C T V T C Q R R K L E K T I Q V GAGGTCTACTCATTCCCTGAAGACCCAGAAATTGAAATAAGTGGA CCACTTGTACACGGGAGACCTGTCACTGTCAACTG CACGGTCCCTAATGTGTACC E V Y S F P E D P E I E I S G P L V H G R P V T V N C T V P N V Y P CCTTTGA CCATCTGGAGATTGAACTACTGAAGGGGGAGACAACACTGTTGAATAAATTTTTAAGGGAGGAAATTGGCACAAAGTCTCTAGAGACCAAAAG F D H L E I E L L K G E T T L L N K F L R E E I G T K S L E T K S TTTGGAAATGACCTTCAT CCCCACCG CTGAAGACACCGGGAAAG CTCTTGTTTG CCTCGCTAAGTTACACAGCAGTCAAATGGAGTCTGAACCCAAACAA L E M T F I P T A E D T G K A L V C L A K L H S S Q M E S E P K Q AGG CAGAGTACACAGACTCTTTATGTCAACGTTGCTCCGAAAGAAC CCACCATCTGGGTTAGCCCCTCTCCTGTCCCAGAGGAGGGCAGTCCTGTGAACC R Q S T Q T L Y V N V A P K E P T I W V S P S P V P E E G S P V N L TGACCTG CTCAAGTGATGGTTTTCCAACTCCCAAAATCCTGTGGAGCAGACAGCTAAAGAACGGGGAACTG CAGCCTCTTTCTCAAAATACAACACT CT C T C S S D G F P T P K I L W S R Q L K N G E L Q P L S Q N T T L S CTTCATGG CTACAAAAATGGAAGATTCCGG CATTTATGTATGTGAAGGGATTAATGAGGCTGGAATTAGCAAAAAATCAGTTGAACTGATTATC CAAGG C F M A T K M E D S G I Y V C E G I N E A G I S K K S V E L I I Q G T•TT•GAAGGACATACAG•TTACAGTCTTCCCATCTAAGAGCGTCAAAGAGGGAGACACTGTCATTATCTCCTGTAcTTGTGGAAGTGTGC•CGAAATAT S S K D I Q L T V F P S K S V K E G D T V I I S C T C G S V P E I W GGATAATTCTGAAAAAGAAAGCCAAGACAGGAGACATGGTGcTAAAGTCTGTTAATGGCTCGTA•AC•ATCCGCAAGGCACAGCTGcAGGATGC•GGAGT I I L K K K A K T G D M V L K S V N G S ¥ T I R K A Q L Q D A G V ATA CGAGTGTGAATCGAAAACCGAAG TCGG CTCG CAGTTGCGAAGTTTAACACTTGATGTGAAAGGAAAAGAAAATAACAAGGACTA'FFFFI'CCCCTGAA Y E C E S K T E V G S Q L R S L T L D V K G K E N N K D Y F S P E CTCCTTG•ACTCTACTTTG•ATCCTCCTTGGTAATACCCGCCATTGGGATGATCATTTACTTTGCAAGAAAAGCCAACATGAAAGGATCATACAGTCTGG L L A L Y F A S S L V I P A I G M I I Y F A R K A N M K G S Y S L V TGGAAGCACAGAAATCAAAAGGGTAGCTAATG E A Q K S K G -
Fig. h Nucleotide and deduced amino acid sequence of rat VCAM-I. SP RABBi THUMANRAT
~
~
~
Tn/CYTO
Fig. 2. Structural homology of the h u m a n , rabbi and rat V C A M - I
a m i n o acid sequences. T h e sequences were aligned by inspection to residues
conserved in the C2 or H type immunoglobulin-like repeats. Cysteine residues forming disulfide bridges in each domain are indicated with arrowheads. Numbers on the left designate the extracellular immunoglobulin domains; SP-signal peptide; T M / C Y T O o t r a n s m e m b r a n e region and cytoplasmic domain.
216
This study was supported by N.1.H. grants HL 45563 (M.C.), HL 36028 (M.C., M. A.G., T.C.) and HL 35716 (T.C.). T.C. is an Established Investigator of the American Heart Association.
4
5
References 6 1 Elices, M.J., Osborn, L., Takada, Y., Crouse, C., Luhowskyj, S., Hemler, M.E. and Lobb, R. (1990) Cell 60, 577-584. 20sborn, L., Hession, C., Tizard, R., Vassalio, C., Luhowskyj, S., Chi-Rosso, G. and Lobb, R. (1989) Cell 59, 1203-1211. 3 Cybulsky, M.I., Fries, J.W.U., Williams, A.J., Sultan, P., Davis,
7
V.M., Gimbrone, M.A., Jr. and Collins, T. (1991) Am. J. Pathol. 138, 815-820. Hession, C., Tizard, R., Vassalo, C., Schiffer, S.G., Goff, D., Moy, P., Chi-Rosso, G., Luhowskyj, S., Lobb, R. and Osborn, L. (1991) J. Biol. Chem. 266, 6682-6685. Polte, T., Newman, W., Raghunathan, G. and Gopal, T.V. (1991) DNA Cell Biol. 10, 349-357. Cybulsky, M.I., Fries, J.W.U., Williams, A.J., Sultan, P., Eddy, R., Byers, M., Shows, T., Gimbrone, M.A., Jr. and Collins, T. (1991) Proc. Nat. Acad. Sci. USA 88, 7859-7863. Hession, C., Moy, P., Tizard, R., Chisohlm, P., Williams, C., Wysk, M., Burkly, L., Miyake, K., Kincade, P. and Lobb, R. (1992) Biochem. Biophys. Res. Commun. 183, t63-169.
Biochimica et Biophysica Acta, 1131 (1992) 214-216 © 1992 Elsevier Science Publishers B.V. All rights reserved 0167-4781/92/$05.00
BBAEXP 90359
Short Sequence-Paper
Nucleotide sequence of rat vascular cell adhesion molecule-1 c D N A A m y J. Williams a Robert C. Atkins b, J o c h e n W.U. Fries a Michael A. G i m b r o n e Jr. a, Myron I. Cybulsky a and Tucker Collins a " Vascular Research Division, Department of Pathology, Brigham and Women's Hospital, Harl,ard Medical School, Boston, MA (USA) and b Department of Nephrology, Monash Medical Center, Clayton (Australia) (Received 27 February 1992)
Key words: Nucleotide sequence; Adhesion molecule-i; (Rat vascular cell)
Vascular cell adhesion molecule 1 (VCAM-1) is an inducible transmembrane protein which is expressed by vascular endothelium following cytokine activation. VCAM-I mediated the adhesion of certain blood leukocytes and tumor cells via the interaction with its counter-receptor, the integrin VLA4 [1]. When initially cloned from interleukin-1 (IL-1) stimulated human umbilical vein endothelial cells, VCAM-1 was reported to contain six immunoglobulin-like domains [2]. However, subsequent cDNA clones [3-5] and structural analysis of the human gene [6] revealed an alternatively spliced seventh immunoglobulin domain. This seven domain form appears to be the predominant transcript in IL-1 activated endothelium [3,4]. In this report, the cloning and nucleotide sequence of rat VCAM-1 is described.
The complete open reading frame of rat VCAM-1 was generated by polymerase chain reaction (PCR) using nested oligonucleotide primers. Total R N A was prepared from lipopolysaccharide treated (4 h) rat lungs by a guanidine isothiocyanate protocol. Reverse transcriptase was used to synthesize first strand c D N A from 1 /.tg of the rat RNA, and three overlapping regions of VCAM-1 c D N A were amplified using three sets of nested P C R primers (four different primers per set). Primers were chosen from regions of the VCAM-1 molecule which contained the greatest degree of conservation based on nucleotide homologies between the human and the rabbit sequences (Cybulskry et al., unpublished data). Three independent clones were sequenced from each of the three nested sets of primers in order to resolve sequence discrepancies due to P C R generated errors.
Correspondence to: T. Collins, Vascular Research Division, Department of Pathology, Brigham and Women's Hospital, 221 Longwood Avenue, Boston, MA 02115, USA.
The c D N A denoted in Fig. 1 has an open reading frame of 2220 base pairs which codes for a protein of 740 amino acids and contains the alternatively spliced domain 4. Rat VCAM-1 showed more than 77% amino acid identity with the rabbit and human proteins (Fig. 2). Like the human form, rat VCAM-1 has internal homology, with domains 1 and 4 being the most homologous (62%). Conservation of this internal repeat is consistent with recent observations that both domains 1 and 4 contain functional binding sites for counter-receptor (Osborn et al., unpublished data). An independent determination of the D N A sequence of a rat VCAM-1 c D N A was recently reported [7]. Two nucleotide differences within the coding region were noted at positions 502 (G to A) and 504 (T to C), which result in a single change in amino acids from Asp to Asn. Sequence analysis of additional rat VCAM-1 cDNAs should reveal whether this is a polymorphism or a P C R generated structural alteration. Since the rat is an important species model for the study of several immune and inflammatory processes, the isolation and characterization of a rat VCAM-1 c D N A will serve as a useful tool to study VCAM-1 pathophysiology.
215 1 101 201 301 401 501 601 701 801 901 i001 1101 1201 1301 1401 1501 1601 1701 1801 1901 2 0 01 2101 2201
TTTAAAATGCCTGGGAAGATGGTCGCGATCTTCGGAG CCTCAACGGTACTTTGGATACTGTTTGCAGTCTCTCAAG CTTTTaAAATCGAGATCTCCCCTG M P G K M V A I F G A S T V L W I L F A V S Q A F K I E I S P E AATACAAAACGCTCGCTCAGATTGGAGACTCCATGCTCCTGACTTGCAGCACCACAGG CTGTGAGTCGCCATCATTCTCTTGGAGAACCCAGATAGACAG ¥ K T L A Q I G D S M L L T C S T T G C E S P S F S W R T Q I D S TCCACTAAATGGGAAGGTGAAGACAGAGGGGGCCAAGTCCGTTCTGACCATGGACCCTGTCAGCTTTGAGAATGAACACTCTTACCTGTGCACAGCAACA P L N G K V K T E G A K S V L T M D P V S F E N E H S ¥ L C T A T TGTAACTCTGGGAAACTGGAAAGAGGAATCCAAGTGGACATCTACTCATTCCCTAAGGATCCAGAGATTCAATTCAGTGGCCCCCTGGAGGTTGGGAAGC C N S G K L E R G I Q V D I Y S F P K D P E I Q F S G P L E V G K P CGGTCATGGTCAAGTGTTTGGCTCCTGATGTTTACCCAATTGACAGACTGGAGATAGAACTGTTCAAGGGTGAC•GTCTCATGAAGAAACAGGATTTTGT V M V K C L A P D V Y P I D R L E I E L F K G D R L M K K Q D F V AAACGAGATGGCAAAGAAGTCTCTGGAAACCAAGAGTTTGGAAGTCATCTTTACTCCTGTCATTGAGGATATTGAAAAGGCTCTTGTTTGCC GAGCTAAA N E M A K K S L E T K S L E V I F T P V I E D I E K A L V C R A K TTATACATTGACCAAACTGATTCTATTCCCAAAGAAAGGGAGACTGTCAGAGAACTACAAGTCTACACCTCCCCCAAGAATACAGAGATCTCTGTACATC L Y I D Q T D S I P K E R E T V R E L Q V ¥ T S P K N T E I S V H P CCTCCACAAGG CTACATGAGGGTG CTGCTGTGACGATGACATGTGCCAG CGAGGGTCTACCAGCTCCTGAGA'FFFI'CTGGAGCAAGAAATTAGATAATGG S T R L H E G A A V T M T C A S E G L P A P E I F W S K K L D N G AGTTCTACAGCTCCTCTCGGGAAATGCCACCCTCACCTTAATTGCTATGAGGATGGAAGATTCTGGAATCTATGTGTGTGAAGGAGTGAATCTGGTTGGG V L Q L L S G N A T L T L I A M R M E D S G I Y V C E G V N L V G AGAGACAAAACAGAAGTGGAATTAATTGTTCAAGAGAAACCATTTACTGTTGACATCTCCC CTGGATCTCAGGTGGCTGCACAGGTTGGGGATTCCGTTG R D K T E V E L I V Q E K P F T V D I S P G S Q V A A Q V G D S V V TTCTGACATGTGCTGCTGTTGGCTGTGACTCTCC CTCC'FFFI'CTTGGAGAACCCAGACAGACAGTCCCCTCAATGGGGAGGTGAGGGATGAAGGGG CTAC L T C A A V G C D S P S F S W R T Q T D S P L N G E V R D E G A T ATCCACACTGACG CTGAG CC CTGTGGGTGTTGAGGATGAGCACTCTTACCTGTGCACTGTGACCTGTCAG CGAAGGAAACTGGAGAAGACAATCCAAGTG S T L T L S P V G V E D E H S ¥ L C T V T C Q R R K L E K T I Q V GAGGTCTACTCATTCCCTGAAGACCCAGAAATTGAAATAAGTGGA CCACTTGTACACGGGAGACCTGTCACTGTCAACTG CACGGTCCCTAATGTGTACC E V Y S F P E D P E I E I S G P L V H G R P V T V N C T V P N V Y P CCTTTGA CCATCTGGAGATTGAACTACTGAAGGGGGAGACAACACTGTTGAATAAATTTTTAAGGGAGGAAATTGGCACAAAGTCTCTAGAGACCAAAAG F D H L E I E L L K G E T T L L N K F L R E E I G T K S L E T K S TTTGGAAATGACCTTCAT CCCCACCG CTGAAGACACCGGGAAAG CTCTTGTTTG CCTCGCTAAGTTACACAGCAGTCAAATGGAGTCTGAACCCAAACAA L E M T F I P T A E D T G K A L V C L A K L H S S Q M E S E P K Q AGG CAGAGTACACAGACTCTTTATGTCAACGTTGCTCCGAAAGAAC CCACCATCTGGGTTAGCCCCTCTCCTGTCCCAGAGGAGGGCAGTCCTGTGAACC R Q S T Q T L Y V N V A P K E P T I W V S P S P V P E E G S P V N L TGACCTG CTCAAGTGATGGTTTTCCAACTCCCAAAATCCTGTGGAGCAGACAGCTAAAGAACGGGGAACTG CAGCCTCTTTCTCAAAATACAACACT CT C T C S S D G F P T P K I L W S R Q L K N G E L Q P L S Q N T T L S CTTCATGG CTACAAAAATGGAAGATTCCGG CATTTATGTATGTGAAGGGATTAATGAGGCTGGAATTAGCAAAAAATCAGTTGAACTGATTATC CAAGG C F M A T K M E D S G I Y V C E G I N E A G I S K K S V E L I I Q G T•TT•GAAGGACATACAG•TTACAGTCTTCCCATCTAAGAGCGTCAAAGAGGGAGACACTGTCATTATCTCCTGTAcTTGTGGAAGTGTGC•CGAAATAT S S K D I Q L T V F P S K S V K E G D T V I I S C T C G S V P E I W GGATAATTCTGAAAAAGAAAGCCAAGACAGGAGACATGGTGcTAAAGTCTGTTAATGGCTCGTA•AC•ATCCGCAAGGCACAGCTGcAGGATGC•GGAGT I I L K K K A K T G D M V L K S V N G S ¥ T I R K A Q L Q D A G V ATA CGAGTGTGAATCGAAAACCGAAG TCGG CTCG CAGTTGCGAAGTTTAACACTTGATGTGAAAGGAAAAGAAAATAACAAGGACTA'FFFFI'CCCCTGAA Y E C E S K T E V G S Q L R S L T L D V K G K E N N K D Y F S P E CTCCTTG•ACTCTACTTTG•ATCCTCCTTGGTAATACCCGCCATTGGGATGATCATTTACTTTGCAAGAAAAGCCAACATGAAAGGATCATACAGTCTGG L L A L Y F A S S L V I P A I G M I I Y F A R K A N M K G S Y S L V TGGAAGCACAGAAATCAAAAGGGTAGCTAATG E A Q K S K G -
Fig. h Nucleotide and deduced amino acid sequence of rat VCAM-I. SP RABBi THUMANRAT
~
~
~
Tn/CYTO
Fig. 2. Structural homology of the h u m a n , rabbi and rat V C A M - I
a m i n o acid sequences. T h e sequences were aligned by inspection to residues
conserved in the C2 or H type immunoglobulin-like repeats. Cysteine residues forming disulfide bridges in each domain are indicated with arrowheads. Numbers on the left designate the extracellular immunoglobulin domains; SP-signal peptide; T M / C Y T O o t r a n s m e m b r a n e region and cytoplasmic domain.
216
This study was supported by N.1.H. grants HL 45563 (M.C.), HL 36028 (M.C., M. A.G., T.C.) and HL 35716 (T.C.). T.C. is an Established Investigator of the American Heart Association.
4
5
References 6 1 Elices, M.J., Osborn, L., Takada, Y., Crouse, C., Luhowskyj, S., Hemler, M.E. and Lobb, R. (1990) Cell 60, 577-584. 20sborn, L., Hession, C., Tizard, R., Vassalio, C., Luhowskyj, S., Chi-Rosso, G. and Lobb, R. (1989) Cell 59, 1203-1211. 3 Cybulsky, M.I., Fries, J.W.U., Williams, A.J., Sultan, P., Davis,
7
V.M., Gimbrone, M.A., Jr. and Collins, T. (1991) Am. J. Pathol. 138, 815-820. Hession, C., Tizard, R., Vassalo, C., Schiffer, S.G., Goff, D., Moy, P., Chi-Rosso, G., Luhowskyj, S., Lobb, R. and Osborn, L. (1991) J. Biol. Chem. 266, 6682-6685. Polte, T., Newman, W., Raghunathan, G. and Gopal, T.V. (1991) DNA Cell Biol. 10, 349-357. Cybulsky, M.I., Fries, J.W.U., Williams, A.J., Sultan, P., Eddy, R., Byers, M., Shows, T., Gimbrone, M.A., Jr. and Collins, T. (1991) Proc. Nat. Acad. Sci. USA 88, 7859-7863. Hession, C., Moy, P., Tizard, R., Chisohlm, P., Williams, C., Wysk, M., Burkly, L., Miyake, K., Kincade, P. and Lobb, R. (1992) Biochem. Biophys. Res. Commun. 183, t63-169.
