A kallikrein-like enzyme in human vascular tissue

Paolo Madeddu, Tiziano Gherli, Pier Paolo Bacciu, Mario Maioli, Nicola Glorioso

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

We attempted to identify the presence of kallikrein in human vascular tissue obtained from patients undergoing surgery. Sections of thoracic (n = 9) and abdominal aorta (n = 6), renal artery (n = 6), and saphenous vein (n = 7) were rinsed with 0.01 mol/ L Tris-HCl buffer, cleaned, minced, and homogenized at 4 °C, The homogenates were centrifuged and supernatants were assayed for protein content and for active and total (trypsin activation) enzymatic activity on the peptide H-d-Val-Leu-Arg-paranitroanilide (S2266), a synthetic substrate for glandular kallikrein. Enzymatic activity was inhibited by aprotinin and polyclonal antibodies against human glandular kallikrein. Kallikrein was resistant to soybean trypsin inhibitor and had an optimum pH of 8.2. A significant correlation was found between the imidolytic and kininogenase activities measured on S2266 and dog kininogen, respectively (r = 0.83, P <.01), The kallikrein-like enzyme was present mainly in the inactive form. Higher levels were found in the homogenates of renal artery (active: 190 ± 36, total: 5036 ± 908 pkat/g protein) than in those of thoracic (active: 38 ± 9, total: 973 ± 350 pkat/g protein) and abdominal aorta (active: 44 ± 10, total: 3031 ± 709 pkat/g protein). In the homogenates of saphenous vein, active and total enzymatic activities averaged 188 ± 90 and 2003 ± 450 pkat/g protein, respectively. A significant inverse correlation was found between the levels of total enzymatic activity in saphenous vein homogenates and mean blood pressure values (r = 0.78, P <.005). These results suggest that a kallikrein-like enzyme is present in human vasculature. Vascular kallikrein might act as a local hormone and regulate regional hemodynamics by releasing kinins.

Original languageEnglish
Pages (from-to)344-348
Number of pages5
JournalAmerican Journal of Hypertension
Volume6
Issue number5 PART 1
Publication statusPublished - May 1993

Fingerprint

Kallikreins
Blood Vessels
Val-Leu-Arg-p-nitroanilide
Saphenous Vein
Enzymes
Tissue Kallikreins
Abdominal Aorta
Renal Artery
Proteins
Thorax
Kininogens
Kinins
Tromethamine
Aprotinin
Trypsin Inhibitors
Soybeans
Trypsin
Hemodynamics
Hormones
Dogs

Keywords

  • arterial blood pressure
  • bradykinin
  • Hypertension
  • kallikrein

ASJC Scopus subject areas

  • Cardiology and Cardiovascular Medicine

Cite this

Madeddu, P., Gherli, T., Bacciu, P. P., Maioli, M., & Glorioso, N. (1993). A kallikrein-like enzyme in human vascular tissue. American Journal of Hypertension, 6(5 PART 1), 344-348.

A kallikrein-like enzyme in human vascular tissue. / Madeddu, Paolo; Gherli, Tiziano; Bacciu, Pier Paolo; Maioli, Mario; Glorioso, Nicola.

In: American Journal of Hypertension, Vol. 6, No. 5 PART 1, 05.1993, p. 344-348.

Research output: Contribution to journalArticle

Madeddu, P, Gherli, T, Bacciu, PP, Maioli, M & Glorioso, N 1993, 'A kallikrein-like enzyme in human vascular tissue', American Journal of Hypertension, vol. 6, no. 5 PART 1, pp. 344-348.
Madeddu P, Gherli T, Bacciu PP, Maioli M, Glorioso N. A kallikrein-like enzyme in human vascular tissue. American Journal of Hypertension. 1993 May;6(5 PART 1):344-348.
Madeddu, Paolo ; Gherli, Tiziano ; Bacciu, Pier Paolo ; Maioli, Mario ; Glorioso, Nicola. / A kallikrein-like enzyme in human vascular tissue. In: American Journal of Hypertension. 1993 ; Vol. 6, No. 5 PART 1. pp. 344-348.
@article{c934dabfdea944699f4de44a5cac2465,
title = "A kallikrein-like enzyme in human vascular tissue",
abstract = "We attempted to identify the presence of kallikrein in human vascular tissue obtained from patients undergoing surgery. Sections of thoracic (n = 9) and abdominal aorta (n = 6), renal artery (n = 6), and saphenous vein (n = 7) were rinsed with 0.01 mol/ L Tris-HCl buffer, cleaned, minced, and homogenized at 4 °C, The homogenates were centrifuged and supernatants were assayed for protein content and for active and total (trypsin activation) enzymatic activity on the peptide H-d-Val-Leu-Arg-paranitroanilide (S2266), a synthetic substrate for glandular kallikrein. Enzymatic activity was inhibited by aprotinin and polyclonal antibodies against human glandular kallikrein. Kallikrein was resistant to soybean trypsin inhibitor and had an optimum pH of 8.2. A significant correlation was found between the imidolytic and kininogenase activities measured on S2266 and dog kininogen, respectively (r = 0.83, P <.01), The kallikrein-like enzyme was present mainly in the inactive form. Higher levels were found in the homogenates of renal artery (active: 190 ± 36, total: 5036 ± 908 pkat/g protein) than in those of thoracic (active: 38 ± 9, total: 973 ± 350 pkat/g protein) and abdominal aorta (active: 44 ± 10, total: 3031 ± 709 pkat/g protein). In the homogenates of saphenous vein, active and total enzymatic activities averaged 188 ± 90 and 2003 ± 450 pkat/g protein, respectively. A significant inverse correlation was found between the levels of total enzymatic activity in saphenous vein homogenates and mean blood pressure values (r = 0.78, P <.005). These results suggest that a kallikrein-like enzyme is present in human vasculature. Vascular kallikrein might act as a local hormone and regulate regional hemodynamics by releasing kinins.",
keywords = "arterial blood pressure, bradykinin, Hypertension, kallikrein",
author = "Paolo Madeddu and Tiziano Gherli and Bacciu, {Pier Paolo} and Mario Maioli and Nicola Glorioso",
year = "1993",
month = "5",
language = "English",
volume = "6",
pages = "344--348",
journal = "American Journal of Hypertension",
issn = "0895-7061",
publisher = "Oxford University Press",
number = "5 PART 1",

}

TY - JOUR

T1 - A kallikrein-like enzyme in human vascular tissue

AU - Madeddu, Paolo

AU - Gherli, Tiziano

AU - Bacciu, Pier Paolo

AU - Maioli, Mario

AU - Glorioso, Nicola

PY - 1993/5

Y1 - 1993/5

N2 - We attempted to identify the presence of kallikrein in human vascular tissue obtained from patients undergoing surgery. Sections of thoracic (n = 9) and abdominal aorta (n = 6), renal artery (n = 6), and saphenous vein (n = 7) were rinsed with 0.01 mol/ L Tris-HCl buffer, cleaned, minced, and homogenized at 4 °C, The homogenates were centrifuged and supernatants were assayed for protein content and for active and total (trypsin activation) enzymatic activity on the peptide H-d-Val-Leu-Arg-paranitroanilide (S2266), a synthetic substrate for glandular kallikrein. Enzymatic activity was inhibited by aprotinin and polyclonal antibodies against human glandular kallikrein. Kallikrein was resistant to soybean trypsin inhibitor and had an optimum pH of 8.2. A significant correlation was found between the imidolytic and kininogenase activities measured on S2266 and dog kininogen, respectively (r = 0.83, P <.01), The kallikrein-like enzyme was present mainly in the inactive form. Higher levels were found in the homogenates of renal artery (active: 190 ± 36, total: 5036 ± 908 pkat/g protein) than in those of thoracic (active: 38 ± 9, total: 973 ± 350 pkat/g protein) and abdominal aorta (active: 44 ± 10, total: 3031 ± 709 pkat/g protein). In the homogenates of saphenous vein, active and total enzymatic activities averaged 188 ± 90 and 2003 ± 450 pkat/g protein, respectively. A significant inverse correlation was found between the levels of total enzymatic activity in saphenous vein homogenates and mean blood pressure values (r = 0.78, P <.005). These results suggest that a kallikrein-like enzyme is present in human vasculature. Vascular kallikrein might act as a local hormone and regulate regional hemodynamics by releasing kinins.

AB - We attempted to identify the presence of kallikrein in human vascular tissue obtained from patients undergoing surgery. Sections of thoracic (n = 9) and abdominal aorta (n = 6), renal artery (n = 6), and saphenous vein (n = 7) were rinsed with 0.01 mol/ L Tris-HCl buffer, cleaned, minced, and homogenized at 4 °C, The homogenates were centrifuged and supernatants were assayed for protein content and for active and total (trypsin activation) enzymatic activity on the peptide H-d-Val-Leu-Arg-paranitroanilide (S2266), a synthetic substrate for glandular kallikrein. Enzymatic activity was inhibited by aprotinin and polyclonal antibodies against human glandular kallikrein. Kallikrein was resistant to soybean trypsin inhibitor and had an optimum pH of 8.2. A significant correlation was found between the imidolytic and kininogenase activities measured on S2266 and dog kininogen, respectively (r = 0.83, P <.01), The kallikrein-like enzyme was present mainly in the inactive form. Higher levels were found in the homogenates of renal artery (active: 190 ± 36, total: 5036 ± 908 pkat/g protein) than in those of thoracic (active: 38 ± 9, total: 973 ± 350 pkat/g protein) and abdominal aorta (active: 44 ± 10, total: 3031 ± 709 pkat/g protein). In the homogenates of saphenous vein, active and total enzymatic activities averaged 188 ± 90 and 2003 ± 450 pkat/g protein, respectively. A significant inverse correlation was found between the levels of total enzymatic activity in saphenous vein homogenates and mean blood pressure values (r = 0.78, P <.005). These results suggest that a kallikrein-like enzyme is present in human vasculature. Vascular kallikrein might act as a local hormone and regulate regional hemodynamics by releasing kinins.

KW - arterial blood pressure

KW - bradykinin

KW - Hypertension

KW - kallikrein

UR - http://www.scopus.com/inward/record.url?scp=0027213432&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027213432&partnerID=8YFLogxK

M3 - Article

VL - 6

SP - 344

EP - 348

JO - American Journal of Hypertension

JF - American Journal of Hypertension

SN - 0895-7061

IS - 5 PART 1

ER -