Pheromone binding by polymorphic mouse major urinary proteins

J 2002

Pheromone binding by polymorphic mouse major urinary proteins

SHARROW, Scott D., Jeffrey L. VAUGHN, Lukáš ŽÍDEK, Milos V. NOVOTNY, Martin J STONE et. al.

Základní údaje

Originální název

Pheromone binding by polymorphic mouse major urinary proteins

Autoři

SHARROW, Scott D. (840 Spojené státy), Jeffrey L. VAUGHN (840 Spojené státy), Lukáš ŽÍDEK (203 Česká republika, garant), Milos V. NOVOTNY (840 Spojené státy) a Martin J STONE (840 Spojené státy)

Vydání

Protein Science, Plainview, Cold Spring Harbor Lab. Press, 2002, 0961-8368

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 3.546

Kód RIV

RIV/00216224:14310/02:00007921

Organizační jednotka

Přírodovědecká fakulta

Klíčová slova anglicky

Binding affinity; isothermal titration calorimetry; major urinary proteins eins; pheromones; selectivity

Štítky

Binding affinity, isothermal titration calorimetry, major urinary proteins eins, pheromones, selectivity

Změněno: 26. 2. 2004 09:58, prof. Mgr. Lukáš Žídek, Ph.D.

Anotace

V originále

Mouse major urinary proteins (MUPs) have been proposed to play a role in regulat ing the release and capture of pheromones. Here, we report affinity measurements of five recombinant urinary MUP isoforms (MUPs-I, II, VII, VIII, and IX) and on e recombinant nasal isoform (MUP-IV) for each of three pheromonal ligands, (+/- )-2-sec-butyl-4,5-dihydrothiazole (SBT), 6-hydroxy-6-methyl-3-heptanone (HMH), a nd (+/-)dehydro-exo-brevicomin (DHB). Dissociation constants for all MUP-pherom one pairs were determined by isothermal titration calorimetry, and data for SBT were corroborated by measurements of intrinsic protein fluorescence. We also rep ort the isolation of MUP-IV protein from mouse nasal extracts, in which MUP-IV m RNA has been observed previously. The affinity of each MUP isoform for SBT (Kd ~ 0.04 to 0.9 uM) is higher than that for DHB (Kd ~ 26 to 58 uM), which in turn is higher than that for HMH (Kd ~ 50 to 200 uM). Isoforms I, II, VIII, a nd IX show very similar affinities for each of the ligands. MUP-VII has approxim ately twofold higher affinity for SBT but approximately twofold lower affinity f or the other pheromones, whereas MUP-IV has ~23-fold higher affinity for SBT and approximately fourfold lower affinity for the other pheromones. The variations in ligand affinities of the MUP isoforms are consistent with structural differen The data indicate that the concentr ations of available pheromones in urine may be influenced by changes in the expr ession levels of urinary MUPs or the excretion levels of other MUP ligands. The variation in pheromone affinities of the urinary MUP isoforms provides only limi ted support for the proposal that MUP heterogeneity plays a role in regulating p rofiles of available pheromones. However, the binding data support the proposed role of nasal MUPs in sequestering pheromones and possibly transporting them to their receptors. ces in the binding cavities of the isoforms.

Návaznosti

GA203/00/0511, projekt VaV

Název: Studium dynamiky a termodynamiky komplexů myších feromonů s proteiny

Investor: Grantová agentura ČR, Studium dynamiky a termodynamiky komplexů myších feromonů s proteiny

Citovat

SHARROW, Scott D., Jeffrey L. VAUGHN, Lukáš ŽÍDEK, Milos V. NOVOTNY a Martin J STONE. Pheromone binding by polymorphic mouse major urinary proteins. Protein Science. Plainview: Cold Spring Harbor Lab. Press, 2002, roč. 11, č. 11, s. 2247-2256. ISSN 0961-8368.

@article{405739,
   author = {Sharrow, Scott D. and Vaughn, Jeffrey L. and Žídek, Lukáš and Novotny, Milos V. and Stone, Martin J},
   article_location = {Plainview},
   article_number = {11},
   keywords = {Binding affinity; isothermal titration calorimetry; major urinary proteins
eins; pheromones; selectivity},
   language = {eng},
   issn = {0961-8368},
   journal = {Protein Science},
   title = {Pheromone binding by polymorphic mouse major urinary proteins},
   volume = {11},
   year = {2002}
}

TY  - JOUR
ID  - 405739
AU  - Sharrow, Scott D. - Vaughn, Jeffrey L. - Žídek, Lukáš - Novotny, Milos V. - Stone, Martin J
PY  - 2002
TI  - Pheromone binding by polymorphic mouse major urinary proteins
JF  - Protein Science
VL  - 11
IS  - 11
SP  - 2247
EP  - 2247
PB  - Cold Spring Harbor Lab. Press
SN  - 09618368
KW  - Binding affinity
KW  - isothermal titration calorimetry
KW  - major urinary proteins
eins
KW  - pheromones
KW  - selectivity
N2  - Mouse major urinary proteins (MUPs) have been proposed to play a role in regulat ing the release and capture of pheromones. Here, we report affinity measurements of five recombinant urinary MUP isoforms (MUPs-I, II, VII, VIII, and IX) and on e recombinant nasal isoform (MUP-IV) for each of three pheromonal ligands, (+/- )-2-sec-butyl-4,5-dihydrothiazole (SBT), 6-hydroxy-6-methyl-3-heptanone (HMH), a nd (+/-)dehydro-exo-brevicomin (DHB). Dissociation constants for all MUP-pherom one pairs were determined by isothermal titration calorimetry, and data for SBT were corroborated by measurements of intrinsic protein fluorescence. We also rep ort the isolation of MUP-IV protein from mouse nasal extracts, in which MUP-IV m RNA has been observed previously. The affinity of each MUP isoform for SBT (Kd ~ 0.04 to 0.9 uM) is higher than that for DHB (Kd ~ 26 to 58 uM), which in turn is higher than that for HMH (Kd ~ 50 to 200 uM). Isoforms I, II, VIII, a nd IX show very similar affinities for each of the ligands. MUP-VII has approxim ately twofold higher affinity for SBT but approximately twofold lower affinity f or the other pheromones, whereas MUP-IV has ~23-fold higher affinity for SBT and approximately fourfold lower affinity for the other pheromones. The variations in ligand affinities of the MUP isoforms are consistent with structural differen The data indicate that the concentr ations of available pheromones in urine may be influenced by changes in the expr ession levels of urinary MUPs or the excretion levels of other MUP ligands. The variation in pheromone affinities of the urinary MUP isoforms provides only limi ted support for the proposal that MUP heterogeneity plays a role in regulating p rofiles of available pheromones. However, the binding data support the proposed role of nasal MUPs in sequestering pheromones and possibly transporting them to their receptors. ces in the binding cavities of the isoforms.
ER  -

SHARROW, Scott D., Jeffrey L. VAUGHN, Lukáš ŽÍDEK, Milos V. NOVOTNY a Martin J STONE. Pheromone binding by polymorphic mouse major urinary proteins. \textit{Protein Science}. Plainview: Cold Spring Harbor Lab. Press, 2002, roč.~11, č.~11, s.~2247-2256. ISSN~0961-8368.

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