Ice t biography released taks

. Author manuscript; available in PMC: 2019 Nov 1.

Published in final edited form as: Hypertension. 2001 Mar;37(3):827–832. doi: 10.1161/01.hyp.37.3.827

Abstract

N-Acetyl-seryl-aspartyl-lysyl-proline (Ac-SDKP) is a natural inhibitor of pluripotent hematopoietic stem cell entry into the S phase of the cell cycle and is normally present in human plasma. Ac-SDKP is exclusively hydrolyzed by ACE, and its plasma concentration is increased 5-fold after ACE inhibition in humans. We examined the effect of 0.05 to 100 nmol/L Ac-SDKP on 24-hour H-thymidine incorporation (DNA synthesis) by cardiac fibroblasts both in the absence and presence of 5% FCS. Captopril (1 μmol/L) was added in all cases to prevent the degradation of Ac-SDKP. Treatment of cardiac fibroblasts with 5% FCS increased thymidine incorporation from a control value of 12 469±594 to 24 598±1051 cpm (P<0.001). Cotreatment with 1 nmol/L Ac-SDKP reduced stimulation to control levels (10 373±200 cpm, P<0.001). We measured hydroxyproline content and incorporation of H-proline into collagenous fibroblast proteins and found that Ac-SDKP blocked endothelin-1 (10 mol/L)–induced collagen synthesis in a biphasic and dose-dependent manner, causing inhibition at low doses, whereas high doses had little or no effect. It also blunted the activity of p44/p42 mitogen-activated protein kinase in a biphasic and dose-dependent manner in serum-stimulated fibroblasts, suggesting that the inhibitory effect of DNA and collagen synthesis may depend in part on blocking mitogen-activated protein kinase activity. Participation of p44/p42 in collagen synthesis was confirmed, because a specific inhibitor for p44/p42 activation (PD 98059, 25 μmol/L) was able to block endothelin-1–induced collagen synthesis, similar to the effect of Ac-SDKP. The fact that Ac-SDKP inhibits DNA and collagen synthesis in cardiac fibroblasts suggests that it may be an important endogenous regulator of fibroblast proliferation and

German battleship Bismarck

German battleship of World War II

Bismarck in 1940

History
Nazi Germany
NameBismarck
NamesakeOtto von Bismarck
BuilderBlohm & Voss, Hamburg
Laid down1 July 1936
Launched14 February 1939
Commissioned24 August 1940
Fate
Badge
General characteristics
Class and typeBismarck-classbattleship
Displacement
Length
  • 241.6 m (792 ft 8 in) waterline
  • 251 m (823 ft 6 in) overall
Beam36 m (118 ft 1 in)
Draft9.3 m (30 ft 6 in) standard
Installed power
  • 12 × Wagner superheated boilers
  • 148,116 shp (110,450 kW)
Propulsion
Speed30.01 knots (55.58 km/h; 34.53 mph) during trials
Range8,870 nmi (16,430 km; 10,210 mi) at 19 knots (35 km/h; 22 mph)
Complement
  • 103 officers
  • 1,962 enlisted men
Sensors and
processing systems
Armament
Armour
  • Belt: 320 mm (12.6 in)
  • Turrets: 360 mm (14.2 in)
  • Main deck: 100–120 mm (3.9–4.7 in)
Aircraft carried4 × Arado Ar 196floatplanes
Aviation facilities1 double-ended catapult

Bismarck was the first of two Bismarck-classbattleships built for Nazi Germany's Kriegsmarine. Named after Chancellor Otto von Bismarck, the ship was laid down at the Blohm & Voss shipyard in Hamburg in July 1936 and launched in February 1939. Work was completed in August 1940, when she was commissioned into the German fleet. Bismarck and her sister ship Tirpitz were the largest battleships ever built by Germany, and two of the largest built by any European power.

In the course of the warship's eight-month career, Bismarck conducted only one offensive operation that lasted eight days in May 1941, codenamed Rheinübung. The ship, along with the heavy cruiserPrinz Eugen, was to break into the Atlantic Ocean and raid Allied shipping

Full-length and N-terminally truncated recombinant interleukin-38 variants are similarly inefficient in antagonizing interleukin-36 and interleukin-1 receptors

  • Brief Report
  • Open access
  • Published:
  • Alejandro Diaz-Barreiro,
  • Dominique Talabot-Ayer,
  • Arnaud Huard,
  • Gea Cereghetti,
  • Jenna Tonacini,
  • Mike Maillasson,
  • Antonio Francés-Monerris,
  • Erwan Mortier &
  • Gaby Palmer

Cell Communication and Signalingvolume 23, Article number: 34 (2025) Cite this article

  • 360 Accesses

  • 2 Altmetric

  • Metrics details

Abstract

Background

Interleukin (IL)-38 is an IL-1 family cytokine that was proposed to exert anti-inflammatory effects. However, its mechanisms of action are not well understood and the identity of the IL-38 receptor(s) remains debated. Proposed candidates include the IL-1 receptor (IL-1R1), the IL-36 receptor (IL-36R) and the orphan receptor IL-1RAPL1. Yet, in literature, IL-38 is often presented as an IL-36R antagonist.

Methods

The N-terminus of the IL-38 protein produced in a human keratinocyte cell line and of endogenous epidermal IL-38 isolated from healthy human skin was characterized by mass spectrometry. The effects of various recombinant forms of IL-38 on IL-36R- and IL-1R1-mediated responses were assessed in IL-36R HEK Blue reporter cells and in a normal human keratinocyte cell line. IL-8 and IL-6 production was quantified by ELISA. Binding of recombinant IL-38 proteins to the IL-36R was assessed by surface plasmon resonance.

Results

Analysis of its native N-terminus revealed that the IL-38 protein produced by human keratinocytes starts at cysteine 2. In cell-based assays, neither full-length amino acid 2-152 IL-38 nor two N-terminally truncated forms of the protein showed efficient antagonist activity on IL-36R- and IL-1R1-mediated responses. The recombinant IL-38 proteins bound to the IL-36R with only moderate affinity, which may provide a mechanistic explanat

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